Yersinia pestis Ail recruitment of C4b-binding protein leads to factor I-mediated inactivation of covalently and noncovalently bound C4b.
作者： Derek K. Ho , Mikael Skurnik , Anna M. Blom , Seppo Meri
关键词: Binding site 、 Complement control protein 、 Biology 、 Biochemistry 、 Complement system 、 Bacterial outer membrane 、 Serine protease 、 C4b-binding protein 、 Yersinia pestis 、 Binding protein 、 Molecular biology
摘要: The outer membrane protein Ail of Yersinia pestis mediates several virulence functions, including serum resistance. Here, we demonstrate that binds C4b-binding (C4BP), the primary fluid-phase regulator classical and lectin pathways. Non-covalent binding C4 C4b to was also observed. C4BP bound can act as a cofactor serine protease factor I (fI) in cleavage C4b. Employing panel alpha-chain mutants, observed absence complement control domain 6 8 reduced Ail. Immunoblot analysis normal human (NHS)-treated bacteria revealed minimal alpha'-chain complexes with bacterial targets. Addition anti-C4BP monoclonal antibody MK104 NHS restored C4b-alpha' chain target complexes, suggesting covalently targets on Y. surface. noncovalently cleaved fI-dependent manner, leaving C4c fragment prevented Collectively, these data suggest when is Ail, fI cleave inactivate has surface structures well
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