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Information on EC 3.4.21.72 - IgA-specific serine endopeptidase
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3.4.21.72 IgA-specific serine endopeptidaseSpecify your search results
Word Map
- 3.4.21.72
- neisseria
- haemophilus
- streptococcus
- influenzae
- gonorrhoeae
- hinge
- meningitidis
- sanguis
-
autotransporter
- pneumococcal
-
gonococcal
-
serogroups
-
meningococci
- oralis
- medicine
-
protease-producing
- lactamica
-
nontypeable
-
paraproteins
- ramosum
-
enzyme-neutralizing
- urealyticum
- pharmacology
- agriculture
- drug development
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
iga1 protease, iga protease, immunoglobulin a1 protease, type 2 iga1 protease, iga1p, iga1-protease, immunoglobulin a protease, iga proteinase, igaa1, iga1-specific protease, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IgA protease
IgA proteinase
-
-
-
-
IgA-specific proteinase
-
-
-
-
IgA1 protease
IgA1-protease
IgA1pr
IgaA1
IgaA2
IgAP
Immunoglobulin A protease
-
-
-
-
Immunoglobulin A proteinase
-
-
-
-
immunoglobulin A1 protease
Proteinase, immunoglobulin A
-
-
-
-
IgA protease
-
-
-
-
IgA1 protease
-
-
-
-
IgA1 protease
Neisseria meningitidis serogroup B B44/76
-
-
-
IgA1-protease
Neisseria meningitidis serogroup B B44/76
-
-
-
IgA1pr
Neisseria meningitidis serogroup B B44/76
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known
cleavage at certain Pro- bonds in the hinge region
-
-
-
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known
the catalytic serine residue is Ser267
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
55127-02-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
degalactosylated IgA1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
desialylated and degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
desialylated/degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fab
-
cleavage of the hinge region
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
IgA proteases only cleave the proline, serine and threonine rich hinge peptide unique to immunoglobulin A1
-
-
?
surface-exposed SD domain + H2O
?
the enzyme cleaves its own isolated recombinant SD domain, single or linked with the alpha-protein, giving the L1 domain
-
-
?
aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
pathogenic human aberrantly glycosylated IgA1
-
-
?
aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
pathogenic human aberrantly glycosylated immunglobulin A1
-
-
?
aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
pathogenic human aberrantly glycosylated IgA1
-
-
?
aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria gonorrhoeae ATCC 49226
-
pathogenic human aberrantly glycosylated IgA1
-
-
?
aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
pathogenic human aberrantly glycosylated IgA1
-
-
?
aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria meningitidis ATCC 13090
-
pathogenic human aberrantly glycosylated IgA1
-
-
?
degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
desialylated and degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
desialylated and degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
desialylated and degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
desialylated IgA1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate
-
-
?
desialylated IgA1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate
-
-
?
desialylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate
-
-
?
desialylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate
-
-
?
human IgA1 + H2O
?
culture supernatants from all strains tested cause degradation of human IgA1
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
the enzyme specifically cleaves the hinge region of human IgA1, the predominant class of immunoglobulin present on mucosal membranes
-
-
?
human IgA1 + H2O
?
unique cleavage specificity of the NTHI IgA1 protease
-
-
?
human IgA1 + H2O
?
deglycosylated human IgA1, the IgA1 protease cleaves two peptide bonds within the human IgA1 hinge region at replicate sequences, cleavage of human IgA1 produces two different sized Fc fragments with N-terminal sequence Thr-Pro-Ser-Pro-Ser
-
-
?
human IgA1 + H2O
?
-
human IgA1 possesses a unique hinge region composed of a repeated sequence rich in proline, serine and threonine, which are the specific cleavage sites of IgA1 protease
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
-
human IgA1 possesses a unique hinge region composed of a repeated sequence rich in proline, serine and threonine, which are the specific cleavage sites of IgA1 protease
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
-
the enzyme possesses a unique substrate specificity to immunoglobulin A1
-
-
?
human IgA1 + H2O
?
-
human IgA1 possesses a unique hinge region composed of a repeated sequence rich in proline, serine and threonine, which are the specific cleavage sites of IgA1 protease
-
-
?
human immunoglobulin A1 + H2O
?
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
-
-
?
human immunoglobulin A1 + H2O
?
site-specific proteolytic cleavage
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human lamp-1 + H2O
?
-
substrate from chang human conjunctiva cells ATCC CCL20.2, human bladder carcinoma cells RT112, JOSK-M cells, DSM ACC30, myelomonocytic cell line, HL60 cells, DSM ACC3, myelocytic cell line
-
?
human lamp-1 + H2O
?
-
substrate from chang human conjunctiva cells ATCC CCL20.2, human bladder carcinoma cells RT112, JOSK-M cells, DSM ACC30, myelomonocytic cell line, HL60 cells, DSM ACC3, myelocytic cell line
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 24% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 27% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 50% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 85% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 21% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 40% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 25% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 25% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 30% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 4% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 30% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 30% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 30% of the substrate is cleaved after 24 h incubation
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma immunglobulin A1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 10211
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 49247
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 49247
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
cleavage of the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria gonorrhoeae ATCC 49226
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria gonorrhoeae ATCC 49226
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria meningitidis ATCC 13090
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria meningitidis ATCC 13090
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
IgA1 from human serum
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
IgA1 from human serum
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
all bacterial IgA1 proteases cleave the heavy chain of IgA1, both serum and secretory IgA2 proteins are IgA1 protease-resistant
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Streptococcus sanguis, Streptococcus pneumoniae and Neisseria gonorrhoeae all release IgA1 proteases each cleaving a single peptide bond, Neisseria meningitidis and Haemophilus influenzae release multiple enzyme types differing in the specific peptide bonds hydrolyzed, e.g. random clinical isolates of Neisseria meningitidis release either type 1 and type 2 protease, type 1 cleaving peptide 237-238 and type 2 cleaving 235-236 in the IgA hinge
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Haemophilus influenzae type 1 enzyme cleaves Pro231-Ser232, type 2 enzyme cleaves Pro235-Thr236, type 3 enzyme cleaves peptide bond 237-238
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
peptide analogs of human IgA as protease substrates
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Haemophilus influenzae enzyme has at least 2 cleavage types. Serogroups, type 1 in serotypes a, b, d, f. Type 2 in c and e
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
human myeloma immunoglobulin
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
all bacterial IgA1 proteases cleave the heavy chain of IgA1, both serum and secretory IgA2 proteins are IgA1 protease-resistant
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Streptococcus sanguis, Streptococcus pneumoniae and Neisseria gonorrhoeae all release IgA1 proteases each cleaving a single peptide bond, Neisseria meningitidis and Haemophilus influenzae release multiple enzyme types differing in the specific peptide bonds hydrolyzed, e.g. random clinical isolates of Neisseria meningitidis release either type 1 and type 2 protease, type 1 cleaving peptide 237-238 and type 2 cleaving 235-236 in the IgA hinge
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
peptide analogs of human IgA as protease substrates
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
specific for human immunoglobulin IgA1
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Neisseria gonorrhoeae cleaves peptide bond 235-236
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
human myeloma immunoglobulin
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
all bacterial IgA1 proteases cleave the heavy chain of IgA1, both serum and secretory IgA2 proteins are IgA1 protease-resistant
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Streptococcus sanguis, Streptococcus pneumoniae and Neisseria gonorrhoeae all release IgA1 proteases each cleaving a single peptide bond, Neisseria meningitidis and Haemophilus influenzae release multiple enzyme types differing in the specific peptide bonds hydrolyzed, e.g. random clinical isolates of Neisseria meningitidis release either type 1 and type 2 protease, type 1 cleaving peptide 237-238 and type 2 cleaving 235-236 in the IgA hinge
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
peptide analogs of human IgA as protease substrates
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
cleaves a Pro-Ser bond in the hinge region of the alpha1 chain between residues 223 and 224
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
specific for human immunoglobulin IgA1
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
all bacterial IgA1 proteases cleave the heavy chain of IgA1, both serum and secretory IgA2 proteins are IgA1 protease-resistant
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Streptococcus sanguis, Streptococcus pneumoniae and Neisseria gonorrhoeae all release IgA1 proteases each cleaving a single peptide bond, Neisseria meningitidis and Haemophilus influenzae release multiple enzyme types differing in the specific peptide bonds hydrolyzed, e.g. random clinical isolates of Neisseria meningitidis release either type 1 and type 2 protease, type 1 cleaving peptide 237-238 and type 2 cleaving 235-236 in the IgA hinge
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
peptide analogs of human IgA as protease substrates
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 36% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 54% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 62% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 71% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
pH 7.2, 37°C, 78% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
pH 7.2, 37°C, 81% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 34% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 34% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 29% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 4% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 17% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 35% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 19% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 22% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
pH 7.2, 37°C, 4% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
pH 7.2, 37°C, 7% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 29% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 29% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 25% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 31% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 19% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 67% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 41% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 51% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
pH 7.2, 37°C, 70% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
pH 7.2, 37°C, 74% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 58% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 20% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 49% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
-
pH 7.2, 37°C, 13% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
-
pH 7.2, 37°C, 14% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
-
pH 7.2, 37°C, 28% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
-
pH 7.2, 37°C, 7% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
pH 7.2, 37°C, 3% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
pH 7.2, 37°C, 7% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
-
pH 7.2, 37°C, 27% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
-
pH 7.2, 37°C, 13% of the substrate is cleaved after 24 h incubation
-
-
?
NF-kappaB p65/RelA component + H2O
?
-
specific cleavage at the C-terminal region of NF-kappaB p65/RelA component within the nucleus of infected cells
-
-
?
NF-kappaB p65/RelA component + H2O
?
-
specific cleavage at the C-terminal region of NF-kappaB p65/RelA component
-
-
?
additional information
?
-
-
in vitro studies show that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes
-
-
?
additional information
?
-
-
the type 2 IgA1 protease is a potential virulence factor in Haemophilus influenzae, the igaB encoded enzyme is the primary mediator of IgA1 protease activity in strain 11P6H, not the type 1 IgA1 protease encoded by igaA, IgA1 proteases are classified as type 1 or type 2 based on the specific site of enzymatic cleavage in the hinge region of the IgA1 molecule
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex
-
-
?
additional information
?
-
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated IgA1 and desialylated/degalactosylated IgA1, as compared to the wild-type IgA1 substrate, while the activity with artificial desialylated IgA1 is reduced
-
-
?
additional information
?
-
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated immunglobulin A1 and desialylated/degalactosylated immunglobulin A1, as compared to the wild-type immunglobulin A1 substrate, while the activity with artificial desialylated immunglobulin A1 is reduced
-
-
?
additional information
?
-
-
the enzyme performs autocatalysis at its autocleavage site
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 10211
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 10211
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 10211
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated IgA1 and desialylated/degalactosylated IgA1, as compared to the wild-type IgA1 substrate, while the activity with artificial desialylated IgA1 is reduced
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 10211
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated immunglobulin A1 and desialylated/degalactosylated immunglobulin A1, as compared to the wild-type immunglobulin A1 substrate, while the activity with artificial desialylated immunglobulin A1 is reduced
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
the enzyme performs autocatalysis at its autocleavage site
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated IgA1 and desialylated/degalactosylated IgA1, as compared to the wild-type IgA1 substrate, while the activity with artificial desialylated IgA1 is reduced
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated immunglobulin A1 and desialylated/degalactosylated immunglobulin A1, as compared to the wild-type immunglobulin A1 substrate, while the activity with artificial desialylated immunglobulin A1 is reduced
-
-
?
additional information
?
-
-
in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated IgA1 and desialylated/degalactosylated IgA1, as compared to the wild-type IgA1 substrate, while the activity with artificial desialylated IgA1 is reduced
-
-
?
additional information
?
-
Neisseria gonorrhoeae ATCC 49226
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Neisseria gonorrhoeae ATCC 49226
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated IgA1 and desialylated/degalactosylated IgA1, as compared to the wild-type IgA1 substrate, while the activity with artificial desialylated IgA1 is reduced
-
-
?
additional information
?
-
-
in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes
-
-
?
additional information
?
-
the NMB IgA1 protease shows a broad substrate specificity for human proteins
-
-
?
additional information
?
-
-
the NMB IgA1 protease shows a broad substrate specificity for human proteins
-
-
?
additional information
?
-
the enzyme performs autoproteolysis at the SD domain
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated IgA1 and desialylated/degalactosylated IgA1, as compared to the wild-type IgA1 substrate, while the activity with artificial desialylated IgA1 is reduced
-
-
?
additional information
?
-
Neisseria meningitidis ATCC 13090
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Neisseria meningitidis ATCC 13090
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated IgA1 and desialylated/degalactosylated IgA1, as compared to the wild-type IgA1 substrate, while the activity with artificial desialylated IgA1 is reduced
-
-
?
additional information
?
-
-
cleavage of p65/RelA occurs at the C-terminal region which contains the transactivation domain (TAD). Removal of the TAD from the rest of the protein may therefore disable the activation capacity of the native p65/RelA molecule
-
-
?
additional information
?
-
-
the enzyme performs autocatalysis at its autocleavage site
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of mutant hhS230P
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fab
-
cleavage of the hinge region
-
-
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
IgA proteases only cleave the proline, serine and threonine rich hinge peptide unique to immunoglobulin A1
-
-
?
NF-kappaB p65/RelA component + H2O
?
-
specific cleavage at the C-terminal region of NF-kappaB p65/RelA component within the nucleus of infected cells
-
-
?
human IgA1 + H2O
?
culture supernatants from all strains tested cause degradation of human IgA1
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
the enzyme specifically cleaves the hinge region of human IgA1, the predominant class of immunoglobulin present on mucosal membranes
-
-
?
human IgA1 + H2O
?
unique cleavage specificity of the NTHI IgA1 protease
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
-
the enzyme possesses a unique substrate specificity to immunoglobulin A1
-
-
?
human immunoglobulin A1 + H2O
?
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 10211
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 49247
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Haemophilus influenzae ATCC 49247
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
cleavage of the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria gonorrhoeae ATCC 49226
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Neisseria meningitidis ATCC 13090
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
IgA1 from human serum
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
IgA1 from human serum
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
additional information
?
-
-
the type 2 IgA1 protease is a potential virulence factor in Haemophilus influenzae, the igaB encoded enzyme is the primary mediator of IgA1 protease activity in strain 11P6H, not the type 1 IgA1 protease encoded by igaA, IgA1 proteases are classified as type 1 or type 2 based on the specific site of enzymatic cleavage in the hinge region of the IgA1 molecule
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 10211
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 10211
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Haemophilus influenzae ATCC 49247
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Neisseria gonorrhoeae ATCC 49226
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
the enzyme performs autoproteolysis at the SD domain
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
Neisseria meningitidis ATCC 13090
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
cleavage of p65/RelA occurs at the C-terminal region which contains the transactivation domain (TAD). Removal of the TAD from the rest of the protein may therefore disable the activation capacity of the native p65/RelA molecule
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(tert-butylamino)-3-[[4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl]oxy]propan-2-ol
-
-
4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl morpholine-4-carboxylate
-
-
4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl piperidine-1-carboxylate
-
-
4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl pyrrolidine-1-carboxylate
-
-
4-(piperidin-1-yl)-1,2,5-thiadiazol-3-yl morpholine-4-carboxylate
-
-
4-methyl-N'-[(morpholin-4-ylcarbonyl)oxy]benzenecarboximidamide
-
-
methyl 3-[([[4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl]oxy]acetyl)amino]benzoate
-
-
N-(1,3-benzodioxol-5-yl)-2-[[4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl]oxy]acetamide
-
-
N-cyclopentyl-2-[[4-(morpholin-4-yl)-1,2,5-thiadiazol-3-yl]oxy]acetamide
-
-
additional information
no inhibition by natural protease inhibitors SLPI, alpha-1-antitrypsin, cathepsin G and cystatin C, and by synthetic protease inhibitors Tos-Lys-chloromethylketone, and ZD0892
-
additional information
-
no inhibition by natural protease inhibitors SLPI, alpha-1-antitrypsin, cathepsin G and cystatin C, and by synthetic protease inhibitors Tos-Lys-chloromethylketone, and ZD0892
-
additional information
-
detection of small molecule, nonpeptidic inhibitors of Haemophilus influenzae IgA1 proteases, inhibitor screening and structure-activity relationship analysis. Improved inhibition and selectivity for IgA protease over other serine proteases
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bacterial Infections
Neisseria gonorrhoeae porin P1.B induces endosome exocytosis and a redistribution of Lamp1 to the plasma membrane.
Behcet Syndrome
IgA protease produced by Streptococcus sanguis and antibody production against IgA protease in patients with Behçet's disease.
Carcinoma, Squamous Cell
Effects of the immunoglobulin A1 protease on Neisseria gonorrhoeae trafficking across polarized T84 epithelial monolayers.
Cholera
C-terminal glycine-histidine tagging of the outer membrane protein Iga beta of Neisseria gonorrhoeae.
Cholera
Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: conformation-dependent outer membrane translocation.
Colitis, Ulcerative
Colonic bacterial proteases to IgA1 and sIgA in patients with ulcerative colitis.
Dental Plaque
Ecology and nature of immunoglobulin A1 protease-producing streptococci in the human oral cavity and pharynx.
Dental Plaque
Evaluation of human oral organisms and pathogenic Streptococcus for production of IgA protease.
Dental Plaque
Of human dental plaque bacteria, Actinomyces viscosus accelerates immunoglobulin A protease secretion in Streptococcus sanguis.
Dental Plaque
The effect of fluoride on Streptococcus sanguis 7863 IgA1 protease production and activity.
Endemic Diseases
Human antibody responses to A and C capsular polysaccharides, IgA1 protease and transferrin-binding protein complex stimulated by infection with Neisseria meningitidis of subgroup IV-1 or ET-37 complex.
Endocarditis, Bacterial
Analysis of the immunoglobulin A protease gene of Streptococcus sanguis.
Gastritis
Increased mucosal production of monomeric IgA1 but no IgA1 protease activity in Helicobacter pylori gastritis.
Glomerulonephritis, IGA
Cloning and Expression of H. influenzae 49247 IgA Protease in E. coli.
Glomerulonephritis, IGA
IgA1 Protease Treatment Reverses Mesangial Deposits and Hematuria in a Model of IgA Nephropathy.
Glomerulonephritis, IGA
Immunoglobulin A1 protease: a new therapeutic candidate for immunoglobulin A nephropathy.
Glomerulonephritis, IGA
Microbial IgA protease removes IgA immune complexes from mouse glomeruli in vivo: potential therapy for IgA nephropathy.
Gonorrhea
Immunoglobulin A1 protease types of Neisseria gonorrhoeae and their relationship to auxotype and serovar.
Gonorrhea
Studies on gonococcus infection. XVII. IgA1-cleaving protease in vaginal washings from women with gonorrhea.
Haemophilus Infections
Nontypeable Haemophilus influenzae in carriage and disease: a difference in IgA1 protease activity levels.
Healthcare-Associated Pneumonia
Cleavage of SIgA by gram negative respiratory pathogens enhance neutrophil inflammatory potential.
Hematuria
IgA1 Protease Treatment Reverses Mesangial Deposits and Hematuria in a Model of IgA Nephropathy.
IgA Deficiency
Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: critical evaluation of experimental evidence.
Infections
A clonal group of nontypeable Haemophilus influenzae with two IgA proteases is adapted to infection in chronic obstructive pulmonary disease.
Infections
A Neisseria gonorrhoeae immunoglobulin A1 protease mutant is infectious in the human challenge model of urethral infection.
Infections
Changes in IgA Protease Expression Are Conferred by Changes in Genomes during Persistent Infection by Nontypeable Haemophilus influenzae in Chronic Obstructive Pulmonary Disease.
Infections
Cleavage of chimpanzee secretory immunoglobulin A by Haemophilus influenzae IgA1 protease.
Infections
Cleavage of SIgA by gram negative respiratory pathogens enhance neutrophil inflammatory potential.
Infections
Differential distribution of IgA-protease genotypes in mucosal and invasive isolates of Haemophilus influenzae in Sweden.
Infections
Electron microscope studies of attachment to human fallopian tube mucosa by a gonococcal IgA1 protease deficient mutant and wild type parent.
Infections
Evaluation of immunoglobulin A1 (IgA1) protease and IgA1 protease-inhibitory activity in human female genital infection with Neisseria gonorrhoeae.
Infections
Expression of IgA Proteases by Haemophilus influenzae in the Respiratory Tract of Adults With Chronic Obstructive Pulmonary Disease.
Infections
Human antibody responses to A and C capsular polysaccharides, IgA1 protease and transferrin-binding protein complex stimulated by infection with Neisseria meningitidis of subgroup IV-1 or ET-37 complex.
Infections
IgA protease production as a characteristic distinguishing pathogenic from harmless neisseriaceae.
Infections
Immunogenicity and evolutionary variability of epitopes within IgA1 protease from serogroup A Neisseria meningitidis.
Infections
Immunoglobulin A Protease Variants Facilitate Intracellular Survival in Epithelial Cells By Nontypeable Haemophilus influenzae That Persist in the Human Respiratory Tract in Chronic Obstructive Pulmonary Disease.
Infections
Immunoglobulin A1 protease types of Neisseria gonorrhoeae and their relationship to auxotype and serovar.
Infections
Immunoglobulin A1 protease, an exoenzyme of pathogenic Neisseriae, is a potent inducer of proinflammatory cytokines.
Infections
Infection of epithelial cells by pathogenic neisseriae reduces the levels of multiple lysosomal constituents.
Infections
Relaxed cleavage specificity of an immunoglobulin A1 protease from Neisseria meningitidis.
Infections
Studies on gonococcus infection. XVI. Purification of Neisseria gonorrhoeae immunoglobulin A1 protease.
Infections
The production and activity in vivo of Proteus mirabilis IgA protease in infections of the urinary tract.
Meningitis, Bacterial
Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: critical evaluation of experimental evidence.
Meningitis, Bacterial
Immunoglobulin A1 protease, an exoenzyme of pathogenic Neisseriae, is a potent inducer of proinflammatory cytokines.
Meningitis, Bacterial
Neisserial immunoglobulin A1 protease induces specific T-cell responses in humans.
Meningitis, Bacterial
Uptake and nuclear transport of Neisseria IgA1 protease-associated alpha-proteins in human cells.
Meningitis, Meningococcal
Antibodies against IgA1 protease are stimulated both by clinical disease and asymptomatic carriage of serogroup A Neisseria meningitidis.
Meningococcal Infections
Invasive isolates of Neisseria meningitidis possess enhanced immunoglobulin A1 protease activity compared to colonizing strains.
Meningococcal Infections
Molecular polymorphism and epidemiology of Neisseria meningitidis immunoglobulin A1 proteases.
Meningococcal Infections
[Protective properties of recombinant IgA1 protease from meningococcus].
Neoplasms
IgA1 protease from Neisseria gonorrhoeae inhibits TNFalpha-mediated apoptosis of human monocytic cells.
Neoplasms
Immunoglobulin A1 protease, an exoenzyme of pathogenic Neisseriae, is a potent inducer of proinflammatory cytokines.
Neoplasms
Neisserial immunoglobulin A1 protease induces specific T-cell responses in humans.
Otitis Media
A clonal group of nontypeable Haemophilus influenzae with two IgA proteases is adapted to infection in chronic obstructive pulmonary disease.
Otitis Media
A single nucleotide polymorphism in an IgA1 protease gene determines Streptococcus pneumoniae adaptation to the middle ear during otitis media.
Otitis Media
Development of antibodies against pneumococcal proteins alpha-enolase, immunoglobulin A1 protease, streptococcal lipoprotein rotamase A, and putative proteinase maturation protein A in relation to pneumococcal carriage and Otitis Media.
Periodontitis
[Protease activity of microflora in the oral cavity of patients with periodontitis]
Persistent Infection
Changes in IgA Protease Expression Are Conferred by Changes in Genomes during Persistent Infection by Nontypeable Haemophilus influenzae in Chronic Obstructive Pulmonary Disease.
Pneumococcal Infections
Production of immunoglobulin A protease by Streptococcus pneumoniae from animals.
Pneumococcal Infections
Protective potency of recombinant meningococcal IgA1 protease and its structural derivatives upon animal invasion with meningococcal and pneumococcal infections.
Pneumonia
Protective potency of recombinant meningococcal IgA1 protease and its structural derivatives upon animal invasion with meningococcal and pneumococcal infections.
Pulmonary Disease, Chronic Obstructive
A clonal group of nontypeable Haemophilus influenzae with two IgA proteases is adapted to infection in chronic obstructive pulmonary disease.
Pulmonary Disease, Chronic Obstructive
Antigenic variation of immunoglobulin A1 proteases among sequential isolates of Haemophilus influenzae from healthy children and patients with chronic obstructive pulmonary disease.
Pulmonary Disease, Chronic Obstructive
Changes in IgA Protease Expression Are Conferred by Changes in Genomes during Persistent Infection by Nontypeable Haemophilus influenzae in Chronic Obstructive Pulmonary Disease.
Pulmonary Disease, Chronic Obstructive
Expression of IgA Proteases by Haemophilus influenzae in the Respiratory Tract of Adults With Chronic Obstructive Pulmonary Disease.
Pulmonary Disease, Chronic Obstructive
Immunoglobulin A Protease Variants Facilitate Intracellular Survival in Epithelial Cells By Nontypeable Haemophilus influenzae That Persist in the Human Respiratory Tract in Chronic Obstructive Pulmonary Disease.
Respiratory Tract Infections
Differential distribution of IgA-protease genotypes in mucosal and invasive isolates of Haemophilus influenzae in Sweden.
Tetanus
IgA protease from Neisseria gonorrhoeae inhibits exocytosis in bovine chromaffin cells like tetanus toxin.
Urethritis
A Neisseria gonorrhoeae immunoglobulin A1 protease mutant is infectious in the human challenge model of urethral infection.
Urethritis
Experimental Gonococcal Infection in Male Volunteers: Cumulative Experience with Neisseria gonorrhoeae Strains FA1090 and MS11mkC.
Urinary Tract Infections
Proteus mirabilis strains of diverse type have IgA protease activity.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the alpha-protein domain has a pI-value of higher than 10
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
non-typeable Haemophilus influenzae, NTHI, gene iga
UniProt
brenda
nontypeable Haemophilus influenzae strains, COPD strains, genes igaA and igaB
-
-
brenda
strain 11P6H, a strain isolated from the sputum of a patient with chronic obstructive pulmonary disease, experiencing an exacerbation, gene igaB
-
-
brenda
Nontypeable Haemophilus influenzae, four IgA1 protease forms: A1, A2, B1, and B2
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
distribution of igaB among clinical isolates of nontypeable Haemophilus influenzae, overview
brenda
additional information
NTHI is a Gram-negative coccobacillus, which colonizes the human upper respiratory tract as part of the normal flora
brenda
additional information
-
NTHI is a Gram-negative coccobacillus, which colonizes the human upper respiratory tract as part of the normal flora
brenda
additional information
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
brenda
additional information
-
bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
inactive pro-enzyme, the cleaved and maturated protein is secreted
brenda
additional information
-
the secreted 150 kDa meningococcal ST-11 IgA protease is carrying nuclear localisation signals (NLS) in its alpha-peptide moiety that allow efficient intranuclear transport in the host cell
-
brenda
active mature enzyme, the cleaved and maturated protein is secreted
-
brenda
-
IgA protease of Neisseria meningitidis consists of an N-terminal signal sequence, a passenger domain and a C-terminal translocator domain that assists in the secretion of the passenger domain across the outer membrane. The protease domain is released into the extracellular milieu either via autocatalytic processing or via cleavage by the autotransporter NalP
brenda
-
IgA protease of Neisseria meningitidis consists of an N-terminal signal sequence, a passenger domain and a C-terminal translocator domain that assists in the secretion of the passenger domain across the outer membrane. The protease domain is released into the extracellular milieu either via autocatalytic processing or via cleavage by the autotransporter NalP
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
Haemophilus influenzae has likely acquired igaB from Neisseria meningitidis, the acquisition is accompanied by a about 20 kb genomic inversion that is present only in strains that have igaB, overview
evolution
-
expression of IgA proteases is variable from strain to strain among NTHi. Analysis of IgA protease expression by 101 persistent strains (median duration of persistence) collected longitudinally from patients enrolled in a 20-year study of COPD upon initial acquisition and immediately before clearance from the host. Upon acquisition, 89 (88%) express IgA protease. A total of 16 of 101 (16%) strains of NTHi alter expression of IgA protease during persistence. Indels and slipped-strand mispairing of mononucleotide repeats confer changes in expression of igaA2. Mechanism of changes in expression, overview
evolution
-
Haemophilus influenzae 49247 IgA protease shows unique DNA and amino acid sequence but with typical endopeptidase domain and beta transporter domain compared to known IgA proteases from the same species
evolution
Haemophilus influenzae ATCC 49247
-
Haemophilus influenzae 49247 IgA protease shows unique DNA and amino acid sequence but with typical endopeptidase domain and beta transporter domain compared to known IgA proteases from the same species
-
malfunction
-
the IgA1/IgA2 ratio is 6.3 for the healthy volunteers and 12.8 for patients with meningitis. IgA2 for the patients with meningitis and the healthy volunteers are almost unchanged, 1:86 and 1:121, respectively
malfunction
-
the IgA1/IgA2 ratio is 6.3 for the healthy volunteers and 12.8 for patients with meningitis. IgA2 for the patients with meningitis and the healthy volunteers are almost unchanged, 1:86 and 1:121, respectively
-
physiological function
Haemophilus influenzae utilizes IgA proteases to aid in defeating the host immune response facilitating disease
physiological function
-
IgA1 protease is a virulence factor of the pathogenic bacterium required for its pathogenesis
physiological function
-
the clonally related group of strains of nontypeable Haemophilus influenzae that has two IgA1 protease genes, iga and igaB, is adapted for colonization and infection in chronic obstructive pulmonary disease, COPD
physiological function
the enzyme performs autoproteolysis at the SD domain, which is important for bacterial adherence to host cells
physiological function
-
ability of IgA1 protease to cleave exclusively IgA1 without affecting IgA2 molecules
physiological function
-
enzyme IgA1P cleaves human immunoglobulin A1 (IgA1), the predominant antibody on human mucosal surfaces. The actions of IgA1Ps impede IgA1 from neutralizing the bacteria. Specifically, IgA1P cleaves IgA1 at a unique hinge region, separating the Fc and Fab fragments of the immunoglobulin. This impairs its Fc-mediated effector response and can even allow bacteria to retain the Fab fragment on their surface in order to mask their polysaccharide capsule and other surface antigens
physiological function
-
IgA1 protease treatment reverses mesangial deposits and hematuria in a model of IgA nephropathy, overview
physiological function
-
nontypeable Haemophilus influenzae (NTHi) expresses four IgA protease variants (A1, A2, B1, and B2) that play different roles in virulence
physiological function
-
nontypeable Haemophilus influenzae (NTHi) expresses four IgA protease variants (A1, A2, B1, and B2) that play different roles in virulence. Expression of IgA protease B2 during persistence in COPD is dynamic and the frequent changes in expression are regulated by slipped-strand mispairing of the igaB2 gene
physiological function
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agIgA1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated IgA1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
physiological function
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agIgA1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated IgA1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
physiological function
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agIgA1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated IgA1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
physiological function
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agimmunglobulin A1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated immunglobulin A1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
physiological function
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex. In addition to be a pathogenic factor, IgA protease is also proven to serve as a potential therapeutic agent in the treatment of IgA nephropathy (IgAN)
physiological function
-
while non-invasive isolates of Neisseria meningitidis (e.g. non-ST-11 isolate LNP19995) provoke a sustained NF-kappaB activation in epithelial cells, hyperinvasive isolates only induce an early NF-kappaB activation followed by a sustained activation of JNK and apoptosis. Elucidation of the mechanism conferring this differential modulation, specifically showing that ST-11 hyperinvasive isolates promote specific cleavage of NF-kappaB p65/RelA component in a secreted IgA protease-dependent manner. This cleavage occurs within the nuclear compartment. Secreted IgA protease from non-invasive isolates is unable to reach the nuclear compartment of infected cells, resulting in a sustained activation of NF-kappaB activity and subsequent cytoprotective effect. Modulation of NF-kappaB-related signaling is likely a double-edged sword to decide the fate of meningococcal infection. Both ST-11 and non-ST-11 isolates cause IkappaBalpha degradation. Meningococcal ST-11 isolates promote nuclear cleavage of p65 at late steps of infection through secreted IgA protease, overview. ST-11 IgA protease-mediated nuclear cleavage of p65/RelA alters selectively expression of NF-kappaB responsive genes in Hec-1-B cells
physiological function
Neisseria gonorrhoeae ATCC 49226
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agIgA1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated IgA1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
-
physiological function
Haemophilus influenzae ATCC 10211
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agIgA1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated IgA1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
-
physiological function
Haemophilus influenzae ATCC 10211
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agimmunglobulin A1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated immunglobulin A1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
-
physiological function
Haemophilus influenzae ATCC 49247
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex. In addition to be a pathogenic factor, IgA protease is also proven to serve as a potential therapeutic agent in the treatment of IgA nephropathy (IgAN)
-
physiological function
Haemophilus influenzae ATCC 49247
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agIgA1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated IgA1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
-
physiological function
Haemophilus influenzae ATCC 49247
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agimmunglobulin A1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated immunglobulin A1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
-
physiological function
-
ability of IgA1 protease to cleave exclusively IgA1 without affecting IgA2 molecules
-
physiological function
-
IgA1 protease is a virulence factor of the pathogenic bacterium required for its pathogenesis
-
physiological function
Neisseria meningitidis ATCC 13090
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agIgA1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated IgA1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
-
additional information
-
IgA1 protease isolated from serogroup A meningococcus is capable of protecting experimental mice infected with meningococcus of serogroup B
additional information
-
the enzyme, isolated from meningococcus serogroup A, is capable of protecting mice infected with meningococcus of serogroup B
additional information
-
immunization of mice with recombinant IgA1 protease of Neisseria meningitidis or several structural derivatives thereof protects the animals infected with a variety of deadly pathogens, including Neisseria meningitidis serogroups A, B, and C and 3 serotypes of Streptococcus pneumonia. In sera of rabbits immunized with inactivated pneumococcal cultures, antibodies binding IgA1-protease from Neisseria meningitidis serogroup B are detected. Cross-reactive protection against meningococcal and pneumococcal infections in vivo
additional information
-
the secreted 150 kDa meningococcal ST-11 IgA protease is carrying nuclear localisation signals (NLS) in its alpha-peptide moiety that allow efficient intranuclear transport in the host Hec-1-B cells
additional information
Neisseria meningitidis serogroup B B44/76
-
immunization of mice with recombinant IgA1 protease of Neisseria meningitidis or several structural derivatives thereof protects the animals infected with a variety of deadly pathogens, including Neisseria meningitidis serogroups A, B, and C and 3 serotypes of Streptococcus pneumonia. In sera of rabbits immunized with inactivated pneumococcal cultures, antibodies binding IgA1-protease from Neisseria meningitidis serogroup B are detected. Cross-reactive protection against meningococcal and pneumococcal infections in vivo
-
Show AA Sequence and Transmembrane Helices (473 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
106000
130000
-
recombinant extracellular His6-tagged IgA protease, gel filtration
additional information
106000
-
Neisseria gonorrhoeae, gel filtration, calculation from gene structure
additional information
-
characterization of the Neisseria IgAbeta-core, the essential unit for outer membrane targeting and extracellular protein secretion
additional information
-
characterization of the Neisseria IgAbeta-core, the essential unit for outer membrane targeting and extracellular protein secretion
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the surface-exposed SD domain, resulting fromn autoproteolysis during autotransportation, of the enzyme is involved in the bacterial adherence to human host epithelial cell surfaces
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
the enzyme performs autocatalysis at its autocleavage site
proteolytic modification
Haemophilus influenzae ATCC 49247
-
the enzyme performs autocatalysis at its autocleavage site
-
proteolytic modification
self-cleavage is required for secretion of the mature extracellular enzyme form, cleavage targets contain a proline-rich consensus recognition sequence, Pro-Pro-Ser-Pro, residing in the variable linker region that connects the protease and translocator domains, the precise amino acid sequence of the intervening region, between mature IgA1 protease and the beta-core translocator domain, influences the efficiency of autoproteolytic processing
proteolytic modification
-
the enzyme performs autocatalysis at its autocleavage site. Proteolytic cleavage of IgA protease may occur at two cleavage sites in ST-11 isolates LNP19995: CS1 autocleavage site (separating the protease domain from the alpha peptide) and CS2 autocleavage site (separating the alpha peptide from the translocator domain). The proteolytic cleavage may occur at the unique CS1 site, leading to release of alpha-peptide-lacking IgA protease in non-ST-11 isolates
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M sodium acetate, pH 5.0, 0.1 M potassium dihydrogen phosphate and 10% (w/v) PEG 20000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P1004A/S1005T/P1006A
site-directed mutagenesis, mutation of the cleavage recognition sequence residues
P1006X
site-directed mutagenesis, mutation of a cleavage recognition sequence residue, the mutant is still able for self-cleavage and subsequent extracellular release of mature IgA1 protease
S1005E
site-directed mutagenesis, mutation of a cleavage recognition sequence residue, the mutant is still able for self-cleavage and subsequent extracellular release of mature IgA1 protease
S267V
site-directed mutagenesis, mutation of the active site catalytic residue, inactive mutant, no self-cleavage and thus no secretion of the enzyme
S267A
additional information
S267A
-
site-directed mutagenesis, catalytically inactive mutant
S267A
-
site-directed mutagenesis, catalytically inactive mutant
-
additional information
-
construction of igaB mutants and igaA/igaB double mutants of strain 11P6H
additional information
construction of deletion or point mutants lacking the previously defined consensus cleavage site, the mutants are still able for self-cleavage and subsequent extracellular release of mature IgA1 protease
additional information
-
construction of deletion or point mutants lacking the previously defined consensus cleavage site, the mutants are still able for self-cleavage and subsequent extracellular release of mature IgA1 protease
additional information
-
creation of four producer strains with effective expression of recombinant proteins (in the form of inclusion bodies) that represent variants of IgA1pr from Neisseria meningitidis serogroup B (strain B44/76) with different primary structures carrying C-terminal histidine label (-LEH6). Protein I is enzymatically active IgA1pr containing M1K2-N963 sequence. Protein IIa (MA28-N963) also possessing specific enzymatic activity is a variant of protein I lacking signal peptide (M1K2-A27). Enzymatically inactive protein IIm is a variant of protein IIa with catalytically active Ser267 residue substituted with an Ala residue. Protein III, a low-molecular-weight fragment of IgA1pr (ME135-H328), is enzymatically inactive and contains a sequence in the IgA1pr region with high density of potential T- and B-cell epitopes
additional information
Neisseria meningitidis serogroup B B44/76
-
creation of four producer strains with effective expression of recombinant proteins (in the form of inclusion bodies) that represent variants of IgA1pr from Neisseria meningitidis serogroup B (strain B44/76) with different primary structures carrying C-terminal histidine label (-LEH6). Protein I is enzymatically active IgA1pr containing M1K2-N963 sequence. Protein IIa (MA28-N963) also possessing specific enzymatic activity is a variant of protein I lacking signal peptide (M1K2-A27). Enzymatically inactive protein IIm is a variant of protein IIa with catalytically active Ser267 residue substituted with an Ala residue. Protein III, a low-molecular-weight fragment of IgA1pr (ME135-H328), is enzymatically inactive and contains a sequence in the IgA1pr region with high density of potential T- and B-cell epitopes
-
additional information
-
generation of an isogenic iga knockout mutant strain, analysis of infection efficiency and persistence in infected cells
additional information
-
construction of an isogenic iga mutant DELTAiga by allelic replacement, which shows significantly decreased lethality to pigs. Removal of gene iga contributes to weakening the ability of Streptoccocus suis in breaking through the mucosa barrier of a host and its inability to invade the pigs
additional information
-
construction of an isogenic iga mutant DELTAiga by allelic replacement, which shows significantly decreased lethality to pigs. Removal of gene iga contributes to weakening the ability of Streptoccocus suis in breaking through the mucosa barrier of a host and its inability to invade the pigs
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, slow loss of activity
Frozen enzyme is stable for at least 1 year
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
development and evaluation of a method for isolation and purification of IgA1 protease from a culture of Neisseria meningitidis serogroup A, purification involves absorption, hydrophobic interaction, anion exchange, and jacalin affinity chromatography steps, to homogeneity, overview
-
native enzyme by hydrophobic interaction chromatography, ultrafiltration, anion exchange chromatography, dialysis, gel filtration, and again ultrafiltration
native enzyme from three inactivated intermediates of meningococcal vaccine production
-
recombinant extracellular His6-tagged IgA protease from Escherichia coli culture medium by nickel affinity chromatography, dialysis, and ultrafiltration, to over 95% purity
-
recombinant His-tagged enzyme variants solubilized from Escherichia coli inclusion bodies by nickel affinity chromatography, dialysis, and anion exchange chromatography
-
recombinant His-tagged IgA1 protease by nickel affinity chromatography, anion exchange chromatography, and gel filtration
recombinant isolated surface-exposed SD domain from Escherichia coli to homogeneity
recombinant refolded enzyme solubilized from Escherichia coli inclusion bodies by ion exchange and hydrophobic interaction chromatography, followed by ultrafiltration and diafiltration
-
native enzyme by hydrophobic interaction chromatography, ultrafiltration, anion exchange chromatography, dialysis, gel filtration, and again ultrafiltration
-
native enzyme by hydrophobic interaction chromatography, ultrafiltration, anion exchange chromatography, dialysis, gel filtration, and again ultrafiltration
-
native enzyme by hydrophobic interaction chromatography, ultrafiltration, anion exchange chromatography, dialysis, gel filtration, and again ultrafiltration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged IgA1 protease in Escherichia coli strain C41(DE3), method development and optimization by evaluation of expression of recombinant Haemophilus influenzae IgA1 protease by combining various expression plasmids, IgA1 protease constructs, and Escherichia coli strains under multiple conditions, overview
expression of the isolated surface-exposed SD domain in Escherichia coli
gene iga, DNA and amino acid sequence determination and analysis
gene iga, DNA and amino acid sequence determination and analysis of NMB IgA1 protease, sequence comparisons, expression of wild-type an dmutant enzymes in Escherichia coli strain XL 1-Blue
gene igaA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, constitutive recombinant expression of codon-optimized gene encoding His6-tagged IgA protease in Escherichia coli and secretion of the enzyme to the culture medium
-
gene igaA, recombinant expression of C-terminally His6-tagged passenger domain of the strains LNP19995 (IgaP-19995) or LNP21019 (IgaP-21019)
-
gene igaB, DNA and amino acid sequence determination and analysis, genetic organization of the igaB locus, overview
-
gene igB2, genotyping and expression analysis, expression of IgA protease B2 varies throughout the duration of persistence. Expression of IgA protease B2 during persistence in COPD is dynamic, and the frequent changes in expression are regulated by slipped-strand mispairing of the igaB2 gene
-
Haemophilus influenzae gene
igaB, COPD strains, DNA sequence determination and analysis, sequence comparisons and relation to strain 11P6H, clonal relationship among the strains, overview
-
Neisseria gonorrhoeae gene in Escherichia coli
recombinant expression of His-tagged enzyme variants in Escherichia coli inclusion bodies
-
recombinant expression of tagged IgA1 protease of Neisseria meningitidis or several structural derivatives thereof, recombinant IgA1pr from Neisseria meningitidis serogroup B strain B44/76 with the primary structure MA28-P1004LEH6 and its N-terminal fragment (protein I, ME135-H328LEH6), proteins II and III are fusion recombinant proteins containing three or two fragments from different regions of base molecule IgA1pr MA28-P1004LEH6. Protein II contains fragments from the N-terminal, central, and C-terminal regions of the base molecule MA28-P1004LEH6, protein III contains fragments from the N-terminal and C-terminal regions of the base molecule
-
recombinant intracellular expression of the enzyme in inclusion bodies in Escherichia coli in fed-batch fermentation
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli inclusion bodies by urea solubilization and refolding
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
drug development
medicine
pharmacology
-
systemically administered IgA protease is able to reduce the quantity of glomerular IgA immune complexes, both the antigen and antibody components, in a passive mouse model of IgA nephropathy
agriculture
-
the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil
agriculture
-
the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil
agriculture
-
the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil
agriculture
-
the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil
analysis
-
the ability of IgA1 protease to cleave exclusively IgA1 without affecting IgA2 molecules allows a more economical and reliable method for determination of these antibody subclasses in human sera based on recombinant Neisseria meningitidis IgA1 protease. Estimation of IgA1 and IgA2 content in human serum and of IgA subclass levels and IgA1/IgA2 ratio using recombinant active and inactive forms of IgA1 protease from Neisseria meningitidis, method evaluation, overview
analysis
-
the ability of IgA1 protease to cleave exclusively IgA1 without affecting IgA2 molecules allows a more economical and reliable method for determination of these antibody subclasses in human sera based on recombinant Neisseria meningitidis IgA1 protease. Estimation of IgA1 and IgA2 content in human serum and of IgA subclass levels and IgA1/IgA2 ratio using recombinant active and inactive forms of IgA1 protease from Neisseria meningitidis, method evaluation, overview
-
drug development
-
a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells
drug development
-
a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells
drug development
-
a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells
drug development
-
a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells
medicine
-
inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces
medicine
-
inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces
medicine
-
inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces
medicine
-
inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces
medicine
-
the inactive mutant E1605A can be considered as a candidate vaccine component
medicine
-
IgA1 protease may be an effective therapeutic candidate for IgAN by removing the mesangial deposited IgA1 in glomerular mesangium leading to immunoglobulin A nephropathy. The removal of IgA1 by IgA1 protease may separate the IgA1-containing immune complexes thereby eliminating its other components at the same time
medicine
-
IgA1 protease may be an effective therapeutic candidate for IgAN by removing the mesangial deposited IgA1 in glomerular mesangium leading to immunoglobulin A nephropathy. The removal of IgA1 by IgA1 protease may separate the IgA1-containing immune complexes thereby eliminating its other components at the same time
medicine
-
IgA1 protease may be an effective therapeutic candidate for IgAN by removing the mesangial deposited IgA1 in glomerular mesangium leading to immunoglobulin A nephropathy. The removal of IgA1 by IgA1 protease may separate the IgA1-containing immune complexes thereby eliminating its other components at the same time
medicine
the IgA1 proteases may have the potential to cleave IgA1 complexes in the human host kidney and be a therapeutic agent for IgA1 nephropathy, a disease characterized by deposition of the IgA1 antibody in the glomerulus
medicine
-
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy
medicine
-
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy
medicine
-
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy
medicine
-
immunization of animals with IgA1pr MA28-P1004LEH6 or proteins I, II, III provides the formation of immunological memory and can protect against both meningococcal and a number of pneumococcal fatal infections. Protective properties of meningococcal IgA1pr MA28-P1004LEH6 and proteins I, II, III against pneumococci may be attributed to their conformational epitopes close in structure to epitopes of pneumococcal surface proteins. In the model of passive animal protection, sera from rabbits immunized with Streptococcus pneumoniae of different serotypes are shown to be capable of animal protection from infection with Neisseria meningitidis, at least serogroup B. Pneumococcal and meningococcal infections can cause a crossprotective effect. This makes meningococcal IgA1 proteases and their recombinant derivatives the potential components of polyvalent vaccines
medicine
Neisseria gonorrhoeae ATCC 49226
-
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy
-
medicine
Haemophilus influenzae ATCC 10211
-
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy
-
medicine
Neisseria meningitidis serogroup B B44/76
-
immunization of animals with IgA1pr MA28-P1004LEH6 or proteins I, II, III provides the formation of immunological memory and can protect against both meningococcal and a number of pneumococcal fatal infections. Protective properties of meningococcal IgA1pr MA28-P1004LEH6 and proteins I, II, III against pneumococci may be attributed to their conformational epitopes close in structure to epitopes of pneumococcal surface proteins. In the model of passive animal protection, sera from rabbits immunized with Streptococcus pneumoniae of different serotypes are shown to be capable of animal protection from infection with Neisseria meningitidis, at least serogroup B. Pneumococcal and meningococcal infections can cause a crossprotective effect. This makes meningococcal IgA1 proteases and their recombinant derivatives the potential components of polyvalent vaccines
-
medicine
Haemophilus influenzae ATCC 49247
-
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy
-
medicine
Neisseria meningitidis ATCC 13090
-
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bachovchin, W.W.; Plaut, A.G.; Flentke, G.R.; Lynch, M.; Kettner, C.A.
Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids
J. Biol. Chem.
265
3738-3743
1990
Haemophilus influenzae, Neisseria gonorrhoeae
brenda
Plaut, A.G.
The IgA1 proteases of pathogenic bacteria
Annu. Rev. Microbiol.
37
603-622
1983
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Streptococcus sanguinis
brenda
Plaut, A.G.; Bachovchin, W.W.
IgA-specific prolyl endopeptidases: serine type
Methods Enzymol.
244
137-151
1994
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Ureaplasma urealyticum
brenda
Grundy, F.J.; Plaut, A.; Wright, A.
Haemophilus influenzae immunoglobulin A1 protease genes: cloning by plasmid integration-excision, comparative analyses, and localization of secretion determinants
J. Bacteriol.
169
4442-4450
1987
Haemophilus influenzae
brenda
Pohlner, J.; Halter, R.; Beyreuther, K.; Meyer, T.F.
Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
Nature
325
458-462
1987
Neisseria gonorrhoeae
brenda
Klauser, T.; Krmer, J.; Otzelberger, K.; Pohlner, J.; Meyer, T.F.
Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion
J. Mol. Biol.
234
579-593
1993
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
brenda
Bleeg, H.S.; Reinholdt, J.; Kilian, M.
Bacterial immunoglobulin A proteases monitored by continuous spectrophotometry
FEBS Lett.
188
357-362
1985
Haemophilus influenzae, Haemophilus influenzae HK 393
brenda
Lindler, L.E.; Stutzenberger, F.J.
Nephelometric assay for the immunoglobulin A1-protease produced by the oral bacterium Streptococcus sanguis
Arch. Oral Biol.
27
853-859
1982
Streptococcus sanguinis
brenda
Mortensen, S.B.; Kilian, M.
Purification and characterization of an immunoglobulin A1 protease from Bacteroides melaninogenicus
Infect. Immun.
45
550-557
1984
Prevotella melaninogenica
brenda
Hauck, C.R.; Meyer, T.F.
The lysosomal/phagosomal membrane protein h-lamp-1 is a target of the IgA1 protease of Neisseria gonorrhoeae
FEBS Lett.
405
86-90
1997
Neisseria gonorrhoeae, no activity in Neisseria gonorrhoeae, no activity in Neisseria gonorrhoeae MS11, Neisseria gonorrhoeae MS11-N139
brenda
Parsons, H.K.; Vitovski, S.; Sayers, J.R.
Immunoglobulin A1 proteases: a structure-function update
Biochem. Soc. Trans.
32
1130-1132
2004
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
brenda
McGillivary, G.; Smoot, L.M.; Actis, L.A.
Characterization of the IgA1 protease from the Brazilian purpuric fever strain F3031 of Haemophilus influenzae biogroup aegyptius
FEMS Microbiol. Lett.
250
229-236
2005
Haemophilus influenzae (Q93T34), Haemophilus influenzae
brenda
Senior, B.W.; Woof, J.M.
Effect of mutations in the human immunoglobulin A1 (IgA1) hinge on its susceptibility to cleavage by diverse bacterial IgA1 proteases
Infect. Immun.
73
1515-1522
2005
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Neisseria meningitidis (Q9K0B4), Streptococcus mitis, Streptococcus oralis, Streptococcus sanguinis, Streptococcus mitis SK599, Streptococcus mitis SK597, Streptococcus oralis SK10, Streptococcus sanguinis SK4, Streptococcus pneumoniae SK690, Streptococcus sanguinis SK1, Streptococcus sanguinis SK49, Streptococcus mitis SK564
brenda
Vidarsson, G.; Overbeeke, N.; Stemerding, A.M.; van den Dobbelsteen, G.; van Ulsen, P.; van der Ley, P.; Kilian, M.; van de Winkel, J.G.
Working mechanism of immunoglobulin A1 (IgA1) protease: cleavage of IgA1 antibody to Neisseria meningitidis PorA requires de novo synthesis of IgA1 Protease
Infect. Immun.
73
6721-6726
2005
Neisseria meningitidis (Q9K0B4), Neisseria meningitidis
brenda
Mistry, D.; Stockley, R.A.
IgA1 protease
Int. J. Biochem. Cell Biol.
38
1244-1248
2006
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
brenda
Bender, M.H.; Weiser, J.N.
The atypical amino-terminal LPNTG-containing domain of the pneumococcal human IgA1-specific protease is required for proper enzyme localization and function
Mol. Microbiol.
61
526-543
2006
Streptococcus pneumoniae
brenda
Romanello, V.; Marcacci, M.; Dal Molin, F.; Moschioni, M.; Censini, S.; Covacci, A.; Baritussio, A.G.; Montecucco, C.; Tonello, F.
Cloning, expression, purification, and characterization of Streptococcus pneumoniae IgA1 protease
Protein Expr. Purif.
45
142-149
2006
Streptococcus pneumoniae
brenda
Fernaays, M.M.; Lesse, A.J.; Cai, X.; Murphy, T.F.
Characterization of igaB, a second immunoglobulin A1 protease gene in nontypeable Haemophilus influenzae
Infect. Immun.
74
5860-5870
2006
Haemophilus influenzae
brenda
Vitovski, S.; Sayers, J.R.
Relaxed cleavage specificity of an immunoglobulin A1 protease from Neisseria meningitidis
Infect. Immun.
75
2875-2885
2007
Neisseria meningitidis (Q51169), Neisseria meningitidis
brenda
Lamm, M.E.; Emancipator, S.N.; Robinson, J.K.; Yamashita, M.; Fujioka, H.; Qiu, J.; Plaut, A.G.
Microbial IgA protease removes IgA immune complexes from mouse glomeruli in vivo: potential therapy for IgA nephropathy
Am. J. Pathol.
172
31-36
2008
Haemophilus influenzae
brenda
Hotomi, M.; Kono, M.; Togawa, A.; Arai, J.; Takei, S.; Ikeda, Y.; Ogami, M.; Murphy, T.F.; Yamanaka, N.
Haemophilus influenzae and Haemophilus haemolyticus in tonsillar cultures of adults with acute pharyngotonsillitis
Auris Nasus Larynx
37
594-600
2010
Haemophilus influenzae, no activity in Haemophilus haemolyticus
brenda
Abuknesha, R.A.; Jeganathan, F.; Wildeboer, D.; Price, R.G.
Optimisation of the detection of bacterial proteases using adsorbed immunoglobulins as universal substrates
Talanta
81
1237-1244
2010
Bacillus licheniformis, Streptomyces griseus
brenda
Pyo, H.M.; Kim, I.J.; Kim, S.H.; Kim, H.S.; Cho, S.D.; Cho, I.S.; Hyun, B.H.
Escherichia coli expressing single-chain Fv on the cell surface as a potential prophylactic of porcine epidemic diarrhea virus
Vaccine
27
2030-2036
2009
Neisseria gonorrhoeae
brenda
Zhang, A.; Mu, X.; Chen, B.; Liu, C.; Han, L.; Chen, H.; Jin, M.
Identification and characterization of IgA1 protease from Streptococcus suis
Vet. Microbiol.
140
171-175
2010
Streptococcus suis
brenda
Johnson, T.A.; Qiu, J.; Plaut, A.G.; Holyoak, T.
Active-site gating regulates substrate selectivity in a chymotrypsin-like serine protease the structure of Haemophilus influenzae IgA1 protease
J. Mol. Biol.
389
559-574
2009
Haemophilus influenzae (P44969), Haemophilus influenzae
brenda
He, S.; Su, Y.; Lin, Y.; Kuo, H.
The surface domain of neisserial IgA1 protease plays a role in induction of bacterial adherence to human epithelial cells
Asian Biomed.
4
231-241
2010
Neisseria meningitidis (Q0PVD3)
-
brenda
Iagudaeva, E.; Zhigis, L.; Razguliaeva, O.; Zueva, V.; Melnikov, E.; Zubov, V.; Kozlov, L.; Bichucher, A.; Kotelnikova, O.; Alliluev, A.; Avakov, A.; Rumsh, L.
Isolation and determination of activity of IgA1 protease from Neisseria meningitidis
Bioorg. Khim.
36
89-97
2010
Neisseria meningitidis
brenda
Long, S.; Phan, E.; Vellard, M.C.
The expression of soluble and active recombinant Haemophilus influenzae IgA1 protease in E. coli
J. Biomed. Biotechnol.
2010
253983
2010
Haemophilus influenzae (P44969), Haemophilus influenzae
brenda
Xie, L.S.; Huang, J.; Qin, W.; Fan, J.M.
Immunoglobulin A1 protease: a new therapeutic candidate for immunoglobulin A nephropathy
Nephrology
15
584-586
2010
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
brenda
Murphy, T.; Lesse, A.; Kirkham, C.; Zhong, H.; Sethi, S.; Munson Jr., R.
A clonal group of nontypeable Haemophilus influenzae with two IgA proteases is adapted to infection in chronic obstructive pulmonary disease
PLoS ONE
6
e25923
2011
Haemophilus influenzae
brenda
Yagudaeva, E.; Zhigis, L.; Razgulyaeva, O.; Zueva, V.; Melnikov, E.; Zubov, V.; Kozlov, L.; Bichucher, A.; Kotelnikova, O.; Alliluev, A.; Avakov, A.; Rumsh, L.
Isolation and determination of the activity of IgA1 protease from Neisseria meningitidis
Russ. J. Bioorg. Chem.
36
81-89
2010
Neisseria meningitidis
brenda
Zhang, A.; Mu, X.; Chen, B.; Han, L.; Chen, H.; Jin, M.
IgA1 protease contributes to the virulence of Streptococcus suis
Vet. Microbiol.
148
436-439
2011
Streptococcus suis, Streptococcus suis 05ZYS
brenda
Mullins, M.A.; Register, K.B.; Bayles, D.O.; Butler, J.E.
Haemophilus parasuis exhibits IgA protease activity but lacks homologs of the IgA protease genes of Haemophilus influenzae
Vet. Microbiol.
153
407-412
2011
Haemophilus influenzae (P44969), Haemophilus influenzae
brenda
Mistry, D.V.; Stockley, R.A.
The cleavage specificity of an IgA1 protease from Haemophilus influenzae
Virulence
2
103-110
2011
Haemophilus influenzae (P44969), Haemophilus influenzae
brenda
Choudary, S.K.; Qiu, J.; Plaut, A.G.; Kritzer, J.A.
Versatile substrates and probes for IgA1 protease activity
ChemBioChem
14
2007-2012
2013
Neisseria gonorrhoeae, Neisseria meningitidis, Neisseria gonorrhoeae MKB, Neisseria meningitidis 1C
brenda
Murphy, T.F.; Kirkham, C.; Jones, M.M.; Sethi, S.; Kong, Y.; Pettigrew, M.M.
Expression of IgA proteases by Haemophilus influenzae in the respiratory tract of adults with chronic obstructive pulmonary disease
J. Infect. Dis.
212
1798-1805
2015
Haemophilus influenzae (N0BM78), Haemophilus influenzae (Q19V48), Haemophilus influenzae, Haemophilus influenzae 124P3H1 (Q19V48), Haemophilus influenzae RD (N0BM78)
brenda
Bek-Thomsen, M.; Poulsen, K.; Kilian, M.
Occurrence and evolution of the paralogous zinc metalloproteases IgA1 protease, ZmpB, ZmpC, and ZmpD in Streptococcus pneumoniae and related commensal species
mBio
3
e00303-12
2012
no activity in Streptococcus suis
brenda
Bek-Thomsen, M.; Poulsen, K.; Kilian, M.
Occurrence and evolution of the paralogous zinc metalloproteases IgA1 protease, ZmpB, ZmpC, and ZmpD in Streptococcus pneumoniae and related commensal species
mBio
3
e00303
2012
no activity in Streptococcus parasanguinis, no activity in Streptococcus cristatus, no activity in Streptococcus oligofermentans, no activity in Streptococcus australis, no activity in Streptococcus peroris, Streptococcus sanguinis (A0A859EML3), Streptococcus sanguinis (F0FDI1), Streptococcus sanguinis (F0FRC4), Streptococcus sanguinis (F0IMK7), Streptococcus sanguinis, Streptococcus mitis (F9MKY1), Streptococcus mitis, Streptococcus sanguinis SK150 (F0IMK7), Streptococcus sanguinis VMC66 (A0A859EML3), Streptococcus sanguinis SK678 (F0FRC4), Streptococcus sanguinis SK353 (F0FDI1), Streptococcus mitis SK569 (F9MKY1)
brenda
Roussel-Jazede, V.; Arenas, J.; Langereis, J.D.; Tommassen, J.; van Ulsen, P.
Variable processing of the IgA protease autotransporter at the cell surface of Neisseria meningitidis
Microbiology
160
2421-2431
2014
Neisseria meningitidis, Neisseria meningitidis H44/76
brenda
Shehaj, L.; Choudary, S.K.; Makwana, K.M.; Gallo, M.C.; Murphy, T.F.; Kritzer, J.A.
Small-molecule inhibitors of Haemophilus influenzae IgA1 protease
ACS Infect. Dis.
5
1129-1138
2019
Haemophilus influenzae NTHI
brenda
Zhigis, L.S.; Kotelnikova, O.V.; Vikhrov, A.A.; Zinchenko, A.A.; Serova, O.V.; Zueva, V.S.; Razgulyaeva, O.A.; Gordeeva, E.A.; Melikhova, T.D.; Nokel, E.A.; Alliluev, A.P.; Drozhzhina, E.Y.; Rumsh, L.D.
A new methodological approach to estimation of IgA1 and IgA2 content in human serum using recombinant IgA1 protease from Neisseria meningitidis
Biotechnol. Lett.
37
2289-2293
2015
Neisseria meningitidis serogroup B, Neisseria meningitidis serogroup B H44/76
brenda
Kotelnikova, O.V.; Zinchenko, A.A.; Vikhrov, A.A.; Alliluev, A.P.; Serova, O.V.; Gordeeva, E.A.; Zhigis, L.S.; Zueva, V.S.; Razgulyaeva, O.A.; Melikhova, T.D.; Nokel, E.A.; Drozhzhina, E.Y.; Rumsh, L.D.
Serological analysis of immunogenic properties of recombinant meningococcus IgA1 protease-based proteins
Bull. Exp. Biol. Med.
161
391-394
2016
Neisseria meningitidis serogroup B, Neisseria meningitidis serogroup B B44/76
brenda
Gallo, M.C.; Kirkham, C.; Eng, S.; Bebawee, R.S.; Kong, Y.; Pettigrew, M.M.; Tettelin, H.; Murphy, T.F.
Changes in IgA protease expression are conferred by changes in genomes during persistent infection by nontypeable Haemophilus influenzae in chronic obstructive pulmonary disease
Infect. Immun.
86
e00313-18
2018
Haemophilus influenzae NTHI
brenda
Lechner, S.M.; Abbad, L.; Boedec, E.; Papista, C.; Le Stang, M.B.; Moal, C.; Maillard, J.; Jamin, A.; Bex-Coudrat, J.; Wang, Y.; Li, A.; Martini, P.G.; Monteiro, R.C.; Berthelot, L.
IgA1 protease treatment reverses mesangial deposits and hematuria in a model of IgA nephropathy
J. Am. Soc. Nephrol.
27
2622-2629
2016
Haemophilus influenzae
brenda
Kotelnikova, O.; Alliluev, A.; Zinchenko, A.; Zhigis, L.; Prokopenko, Y.; Nokel, E.; Razgulyaeva, O.; Zueva, V.; Tokarskaya, M.; Yastrebova, N.; Gordeeva, E.; Melikhova, T.; Kaliberda, E.; Rumsh, L.
Protective potency of recombinant meningococcal IgA1 protease and its structural derivatives upon animal invasion with meningococcal and pneumococcal infections
Microbes Infect.
21
336-340
2019
Neisseria meningitidis serogroup B, Neisseria meningitidis serogroup B B44/76
brenda
Wang, H.; Zhong, X.; Li, J.; Zhu, M.; Wang, L.; Ji, X.; Fan, J.; Wang, L.
Cloning and expression of H. influenzae 49247 IgA protease in E. coli
Mol. Biotechnol.
60
134-140
2018
Haemophilus influenzae, Haemophilus influenzae ATCC 49247
brenda
Besbes, A.; Le Goff, S.; Antunes, A.; Terrade, A.; Hong, E.; Giorgini, D.; Taha, M.K.; Deghmane, A.E.
Hyperinvasive meningococci induce intra-nuclear cleavage of the NF-kappaB protein p65/RelA by meningococcal IgA protease
PLoS Pathog.
11
e1005078
2015
Neisseria meningitidis serogroup C
brenda
Wang, L.; Li, X.; Shen, H.; Mao, N.; Wang, H.; Cui, L.; Cheng, Y.; Fan, J.
Bacterial IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes as a potential therapy for IgA nephropathy
Sci. Rep.
6
30964
2016
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Neisseria gonorrhoeae ATCC 49226, Haemophilus influenzae ATCC 10211, Haemophilus influenzae ATCC 49247, Neisseria meningitidis ATCC 13090
brenda
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