3.4.21.72: IgA-specific serine endopeptidase
This is an abbreviated version!
For detailed information about IgA-specific serine endopeptidase, go to the full flat file.
Word Map on EC 3.4.21.72
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3.4.21.72
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neisseria
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haemophilus
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streptococcus
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influenzae
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gonorrhoeae
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hinge
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meningitidis
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sanguis
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autotransporter
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pneumococcal
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gonococcal
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serogroups
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meningococci
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oralis
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medicine
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protease-producing
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lactamica
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nontypeable
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paraproteins
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ramosum
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enzyme-neutralizing
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urealyticum
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pharmacology
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agriculture
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drug development
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analysis
- 3.4.21.72
- neisseria
- haemophilus
- streptococcus
- influenzae
- gonorrhoeae
- hinge
- meningitidis
- sanguis
-
autotransporter
- pneumococcal
-
gonococcal
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serogroups
-
meningococci
- oralis
- medicine
-
protease-producing
- lactamica
-
nontypeable
-
paraproteins
- ramosum
-
enzyme-neutralizing
- urealyticum
- pharmacology
- agriculture
- drug development
- analysis
Reaction
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known =
Synonyms
Iga, IgA protease, IgA protease A1, IgA protease B2, IgA proteinase, IgA-specific proteinase, IgA1 protease, IgA1-protease, IgA1-specific protease, IgA1?P, IgA1P, IgA1pr, IgaA1, IgaA2, IgaB2, IgAP, Immunoglobulin A protease, Immunoglobulin A proteinase, immunoglobulin A1 protease, NMB IgA1 protease, Proteinase, immunoglobulin A, serine-type IgA1 protease, serine-type immunoglobulin A1 protease, ST-11 IgA protease, type 2 IgA1 protease
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General Information
General Information on EC 3.4.21.72 - IgA-specific serine endopeptidase
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evolution
malfunction
physiological function
additional information
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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
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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
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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
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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
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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
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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
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Haemophilus influenzae utilizes IgA proteases to aid in defeating the host immune response facilitating disease
physiological function
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IgA1 protease is a virulence factor of the pathogenic bacterium required for its pathogenesis
physiological function
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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
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ability of IgA1 protease to cleave exclusively IgA1 without affecting IgA2 molecules
physiological function
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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
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IgA1 protease treatment reverses mesangial deposits and hematuria in a model of IgA nephropathy, overview
physiological function
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nontypeable Haemophilus influenzae (NTHi) expresses four IgA protease variants (A1, A2, B1, and B2) that play different roles in virulence
physiological function
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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
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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
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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
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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
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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
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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
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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
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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
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physiological function
Haemophilus influenzae ATCC 10211
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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
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physiological function
Haemophilus influenzae ATCC 10211
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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
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physiological function
Haemophilus influenzae ATCC 49247
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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
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physiological function
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ability of IgA1 protease to cleave exclusively IgA1 without affecting IgA2 molecules
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physiological function
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IgA1 protease is a virulence factor of the pathogenic bacterium required for its pathogenesis
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physiological function
Neisseria meningitidis ATCC 13090
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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
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IgA1 protease isolated from serogroup A meningococcus is capable of protecting experimental mice infected with meningococcus of serogroup B
additional information
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the enzyme, isolated from meningococcus serogroup A, is capable of protecting mice infected with meningococcus of serogroup B
additional information
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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
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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
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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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