3.4.24.13: IgA-specific metalloendopeptidase
This is an abbreviated version!
For detailed information about IgA-specific metalloendopeptidase, go to the full flat file.
Word Map on EC 3.4.24.13
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3.4.24.13
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medicine
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hinge
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gonorrhoeae
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influenzae
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haemophilus
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proteinases
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neisserial
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20-year
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colostrum
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nontypeable
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fcalpha
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hexxh
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meningitidis
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airways
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tetrapeptide
- 3.4.24.13
- medicine
- hinge
- gonorrhoeae
- influenzae
-
haemophilus
- proteinases
-
neisserial
-
20-year
-
colostrum
-
nontypeable
- fcalpha
-
hexxh
- meningitidis
- airways
- tetrapeptide
Reaction
Cleavage of Pro-/-Thr bond in the hinge region of the heavy chain of human IgA =
Synonyms
HP1022, Iga, IgA protease, IgA protease A2, IgA protease B1, IgA1 protease, IgA1 proteinase, IgA1-protease, IgA1-specific proteinase, IgA1P, IgA1pr, igA2, IgaA2, igaB, igaB1, IgaB2, immunoglobulin A1 protease, proteinase, immunoglobulin A1, Streptococcus pneumoniae IgA1 protease, zinc metalloprotease zmpC
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General Information
General Information on EC 3.4.24.13 - IgA-specific metalloendopeptidase
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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
physiological function
additional information
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IgA1 protease may play an important role in the pathogenesis of Streptococcus suis
physiological function
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the enzyme catalyzes the proteolysis of human IgA1 at its hinge region to leave the bacterial cell surface masked by IgA1 Fab, enabling the bacteria to evade the host's immune system and adhere to host epithelial cells to promote colonization
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 (IgA1P) specifically cleaves human immunoglobulin A1 (IgA1) at the hinge region dissociating the effector Fc region while the IgA1 FAB remains bound to the bacterial surface. This cleavage promotes infection by two mechanisms. Firstly, Fc receptors on neutrophils can no longer recognize the cleaved and released IgA1 Fc to bind and kill the bacterial cells. Secondly, the IgA1 FAB fragment remaining on the Streptococcus pneumoniae cell surface enhances Streptococcus pneumoniae binding to epithelial cells and can no longer prevent colonization
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
the virulence-associated protein, IgA1 protease, is a surface protective antigen of SS2
physiological function
Streptococcus suis DAT1 SC-19
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the virulence-associated protein, IgA1 protease, is a surface protective antigen of SS2
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physiological function
Streptococcus suis DAT1 ZYS
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the virulence-associated protein, IgA1 protease, is a surface protective antigen of SS2
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physiological function
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IgA1 protease may play an important role in the pathogenesis of Streptococcus suis
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IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a BALB/c mouse model
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 Neissseria 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 conserved HExxH motif (amino acid residues 1604-1608) coordinates Zn2+ and provides the catalytic base, Glu1605. Residue Glu1628 also contributes to IgA1P catalytic activity. The C-terminal domain, IgA1P1612-1963, exhibits no detectable binding to IgA1. The Streptococcus pneumoniae IgA1P N- and C-terminal regions are catalytically active when combined in trans
additional information
Streptococcus suis DAT1 SC-19
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IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a BALB/c mouse model
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additional information
Streptococcus suis DAT1 ZYS
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IgA1 protease is a surface protective antigen of Streptococcus suis serotype 2 (SS2), immunization with purified recombinant IgA1 protease (amino acid residues 600-1926) induces high IgG antibody titers and confers complete protection against a challenge with a lethal dose of SS2 in a BALB/c mouse model
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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 Neissseria 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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