EC Number   |
General Information |
Reference |
|---|
   3.4.24.13 | 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 |
753802 |
| 3.4.24.13 | more |
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 |
-, 754643 |
| 3.4.24.13 | more |
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 |
-, 754644 |
| 3.4.24.13 | more |
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 |
755335 |
| 3.4.24.13 | 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 |
752366 |
| 3.4.24.13 | physiological function |
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 |
755335 |
| 3.4.24.13 | physiological function |
IgA1 protease may play an important role in the pathogenesis of Streptococcus suis |
-, 710668 |
| 3.4.24.13 | physiological function |
nontypeable Haemophilus influenzae (NTHi) expresses four IgA protease variants (A1, A2, B1, and B2) that play different roles in virulence |
753802 |
| 3.4.24.13 | physiological function |
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 |
731982 |
| 3.4.24.13 | physiological function |
the virulence-associated protein, IgA1 protease, is a surface protective antigen of SS2 |
-, 754643 |
