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10.1042/BJ20141069 http://scihub22266oqcxt.onion/10.1042/BJ20141069 C5600146!5600146!25330773     free     free     free Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 249.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+J 2015 ; 465 (2): 325-35 Nephropedia Template TP {{tp|p=25330773|t=2015. Structural Determinants of Host Specificity of Complement Factor H Recruitment by Streptococcus pneumoniae |pdf=|usr=}}{{25330773}} gab.com Text Structural Determinants of Host Specificity of Complement Factor H Recruitment by Streptococcus pneumoniae JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=25330773 #FOAvip 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. Twit Text FOAVip Structural Determinants of Host Specificity of Complement Factor H Recruitment by Streptococcus pneumoniae ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=25330773 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25330773 #FOAvip English Wikipedia <ref>{{Cite pmid|25330773}}</ref> Structural Determinants of Host Specificity of Complement Factor H Recruitment by Streptococcus pneumoniae #MMPMID25330773 Achila D; Liu A; Banerjee R; Li Y; Martinez-Hackert E; Zhang JR; Yan H Biochem J 2015[Jan]; 465 (2): 325-35 PMID25330773show ga 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. äStructural Determinants of Host Specificity of Complement Factor H Rec(epmc).pdf DeepDyve Pubget Overpricing