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- W1805590927 abstract "The outer membrane protein A il of Y ersinia pestis mediates several virulence functions, including serum resistance. Here, we demonstrate that A il binds C 4b‐binding protein ( C 4 BP ), the primary fluid‐phase regulator of the classical and lectin pathways. Non‐covalent binding of C 4 and C 4b to A il was also observed. C 4 BP bound to A il can act as a cofactor to the serine protease factor I (fI) in the cleavage of fluid‐phase C 4b. Employing a panel of C 4 BP alpha‐chain mutants, we observed that the absence of complement control protein domain 6 and 8 reduced binding to Ail. Immunoblot analysis of normal human serum ( NHS )‐treated bacteria revealed minimal C 4b alpha’‐chain complexes with bacterial outer membrane targets. Addition of the anti‐ C 4 BP monoclonal antibody MK 104 to NHS restored C 4b‐alpha’ chain target complexes, suggesting that C 4b binds covalently to targets on the Y. pestis surface. C4b bound to A il noncovalently was also cleaved in a C 4 BP and fI‐dependent manner, leaving the C 4c fragment bound to A il. MK 104 also prevented the cleavage of noncovalently bound C 4b. Collectively, these data suggest that when C 4 BP is bound to A il, fI can cleave and inactivate C 4b that has bound covalently to bacterial surface structures as well as C 4b bound noncovalently to A il." @default.
- W1805590927 created "2016-06-24" @default.
- W1805590927 creator A5025820462 @default.
- W1805590927 creator A5060352582 @default.
- W1805590927 creator A5068835834 @default.
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- W1805590927 date "2014-01-13" @default.
- W1805590927 modified "2023-10-16" @default.
- W1805590927 title "<i>Yersinia pestis</i>Ail recruitment of C4b-binding protein leads to factor I-mediated inactivation of covalently and noncovalently bound C4b" @default.
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- W1805590927 doi "https://doi.org/10.1002/eji.201343552" @default.
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