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aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
degalactosylated IgA1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
desialylated and degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
desialylated IgA1 + H2O
immunglobulin Fc + immunglobulin Fd
desialylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
desialylated/degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
human immunoglobulin A1 + H2O
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
IgA2-IgA1 half hinge + H2O
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fab
-
cleavage of the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
Immunoglobulin A1 + H2O
?
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
IgA proteases only cleave the proline, serine and threonine rich hinge peptide unique to immunoglobulin A1
-
-
?
mutant hhS224/230P + H2O
?
NF-kappaB p65/RelA component + H2O
?
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
-
-
?
additional information
?
-
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
-
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
-
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
?
-
-
-
?
human IgA1 + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
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
-
?
IgA + H2O
?
-
-
-
-
?
IgA1 + H2O
?
-
-
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
IgA1 + H2O
?
-
pH 7.2, 37°C
-
-
?
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
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
cleavage of the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
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
?
-
-
-
?
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 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 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
-
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
-
?
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
-
-
?
porcine IgA1 + H2O
?
-
-
-
-
?
porcine IgA1 + H2O
?
-
-
-
-
?
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
?
-
no activity with human IgA2
-
-
?
additional information
?
-
-
no activity with human IgA2
-
-
?
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
?
-
-
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 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 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 performs autocatalysis at its autocleavage site
-
-
?
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 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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
?
additional information
?
-
-
no cleavage of IgA2
-
-
?
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
?
-
-
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
?
-
-
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 mutant hhS230P
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of mutant hhS230P
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of mutant hhS230P
-
-
?
additional information
?
-
-
no cleavage of IgA2-IgA1 half hinge, mutants hhS230P, hhS224P, hhS224/230P, hhP227S
-
-
?
additional information
?
-
-
no cleavage of mutant hhS230P
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
human immunoglobulin A1 + H2O
?
human immunoglobulin A1 + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fab
-
cleavage of the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
Immunoglobulin A1 + H2O
?
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
-
-
?
additional information
?
-
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
?
-
-
-
-
?
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
-
-
-
-
?
IgA1 + H2O
?
-
-
-
-
?
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
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
cleavage of the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
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
?
-
-
-
-
?
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 A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
Immunoglobulin A1 + H2O
?
-
-
-
?
porcine IgA1 + H2O
?
-
-
-
-
?
porcine IgA1 + H2O
?
-
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bacteremia
Pneumococcal IgA1 protease subverts specific protection by human IgA1.
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.
Blister
Gonococci are survivors.
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 Caries
Analysis of the immunoglobulin A protease gene of Streptococcus sanguis.
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
Lack of immunoglobulin A1 protease production by Branhamella catarrhalis.
Infections
Pneumococcal IgA1 protease subverts specific protection by human IgA1.
Infections
Proteus mirabilis strains of diverse type have IgA protease activity.
Infections
Relaxed cleavage specificity of an immunoglobulin A1 protease from Neisseria meningitidis.
Infections
Secretory immunity and the bacterial IgA proteases.
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
[Clinical significance of analysis of immunoglobulin A levels in saliva]
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
Immunoglobulin A protease is a virulence factor for gram-negative pneumonia.
Pneumonia
Production of immunoglobulin A protease by Streptococcus pneumoniae from animals.
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.
Whooping Cough
[IgA protease activity of microbes in the genus Bordetella]
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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 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
-
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
-
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
-
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
-
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
-
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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