Structural highlights
Publication Abstract from PubMed
Many human pathogens have strict host specificity, which affects not only their epidemiology but also development of animal models and vaccines. Complement factor H (FH) is recruited to pneumococcal cell surface in a human-specific manner via the N-terminal domain of the pneumococcal protein virulence factor CbpA (CbpAN). FH recruitment enables Streptococcus pneumoniae to evade surveillance by human complement system and contributes to pneumococcal host specificity. The molecular determinants of host specificity of complement evasion are unknown. Here we show that a single human FH domain is sufficient for tight binding of CbpAN, present the crystal structure of the complex, and identify the critical structural determinants for host-specific FH recruitment. The results offer new approaches to development of better animal models for pneumococcal infection and redesign of the virulence factor for pneumococcal vaccine development, and reveal how FH recruitment can serve as a mechanism for both pneumococcal complement evasion and adherence.
Structural Determinants of Host Specificity of Complement Factor H Recruitment by Streptococcus pneumoniae.,Achila D, Liu A, Banerjee R, Li Y, Martinez-Hackert E, Zhang JR, Yan H Biochem J. 2014 Oct 21. PMID:25330773[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Achila D, Liu A, Banerjee R, Li Y, Martinez-Hackert E, Zhang JR, Yan H. Structural Determinants of Host Specificity of Complement Factor H Recruitment by Streptococcus pneumoniae. Biochem J. 2014 Oct 21. PMID:25330773 doi:http://dx.doi.org/10.1042/BJ20141069
