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10.1074/jbc.M114.630871 http://scihub22266oqcxt.onion/10.1074/jbc.M114.630871 C4392255!4392255 !25659429     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25659429 &cmd=llinks): Failed to open stream: HTTP request failed! 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The major autoantibody epitope on factor H in atypical hemolytic uremic syndrome is structurally different from its homologous site in factor H-related protein 1, supporting a novel model for induction of autoimmunity in this disease |pdf=|usr=}}{{25659429 }} gab.com Text The major autoantibody epitope on factor H in atypical hemolytic uremic syndrome is structurally different from its homologous site in factor H-related protein 1, supporting a novel model for induction of autoimmunity in this disease JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25659429 #FOAvip Atypical hemolytic uremic syndrome (aHUS) is characterized by complement attack against host cells due to mutations in complement proteins or autoantibodies against complement factor H (CFH). It is unknown why nearly all patients with autoimmune aHUS lack CFHR1 (CFH-related protein-1). These patients have autoantibodies against CFH domains 19 and 20 (CFH19-20), which are nearly identical to CFHR1 domains 4 and 5 (CFHR14-5). Here, binding site mapping of autoantibodies from 17 patients using mutant CFH19-20 constructs revealed an autoantibody epitope cluster within a loop on domain 20, next to the two buried residues that are different in CFH19-20 and CFHR14-5. The crystal structure of CFHR14-5 revealed a difference in conformation of the autoantigenic loop in the C-terminal domains of CFH and CFHR1, explaining the variation in binding of autoantibodies from some aHUS patients to CFH19-20 and CFHR14-5. The autoantigenic loop on CFH seems to be generally flexible, as its conformation in previously published structures of CFH19-20 bound to the microbial protein OspE and a sialic acid glycan is somewhat altered. Cumulatively, our data suggest that association of CFHR1 deficiency with autoimmune aHUS could be due to the structural difference between CFHR1 and the autoantigenic CFH epitope, suggesting a novel explanation for CFHR1 deficiency in the pathogenesis of autoimmune aHUS. Twit Text FOAVip The major autoantibody epitope on factor H in atypical hemolytic uremic syndrome is structurally different from its homologous site in factor H-related protein 1, supporting a novel model for induction of autoimmunity in this disease ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25659429 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25659429 #FOAvip English Wikipedia <ref>{{Cite pmid|25659429 }}</ref> The major autoantibody epitope on factor H in atypical hemolytic uremic syndrome is structurally different from its homologous site in factor H-related protein 1, supporting a novel model for induction of autoimmunity in this disease #MMPMID25659429 Bhattacharjee A ; Reuter S ; Trojnár E ; Kolodziejczyk R ; Seeberger H ; Hyvärinen S ; Uzonyi B ; Szilágyi Á ; Prohászka Z ; Goldman A ; Józsi M ; Jokiranta TS J Biol Chem 2015[Apr]; 290 (15 ): 9500-10 PMID25659429 show ga Atypical hemolytic uremic syndrome (aHUS) is characterized by complement attack against host cells due to mutations in complement proteins or autoantibodies against complement factor H (CFH). It is unknown why nearly all patients with autoimmune aHUS lack CFHR1 (CFH-related protein-1). These patients have autoantibodies against CFH domains 19 and 20 (CFH19-20), which are nearly identical to CFHR1 domains 4 and 5 (CFHR14-5). Here, binding site mapping of autoantibodies from 17 patients using mutant CFH19-20 constructs revealed an autoantibody epitope cluster within a loop on domain 20, next to the two buried residues that are different in CFH19-20 and CFHR14-5. The crystal structure of CFHR14-5 revealed a difference in conformation of the autoantigenic loop in the C-terminal domains of CFH and CFHR1, explaining the variation in binding of autoantibodies from some aHUS patients to CFH19-20 and CFHR14-5. The autoantigenic loop on CFH seems to be generally flexible, as its conformation in previously published structures of CFH19-20 bound to the microbial protein OspE and a sialic acid glycan is somewhat altered. Cumulatively, our data suggest that association of CFHR1 deficiency with autoimmune aHUS could be due to the structural difference between CFHR1 and the autoantigenic CFH epitope, suggesting a novel explanation for CFHR1 deficiency in the pathogenesis of autoimmune aHUS. |Atypical Hemolytic Uremic Syndrome/genetics/immunology/metabolism [MESH] |Autoantibodies/*chemistry/immunology [MESH] |Autoimmunity/genetics/immunology [MESH] |Binding Sites/genetics/immunology [MESH] |Complement C3b Inactivator Proteins/*chemistry/genetics/immunology [MESH] |Complement Factor H/*chemistry/genetics/immunology [MESH] |Crystallography, X-Ray [MESH] |Epitope Mapping [MESH] |Epitopes/*chemistry/immunology [MESH] |Humans [MESH] |Models, Molecular [MESH] |Mutation [MESH] |Peptide Fragments/chemistry/immunology [MESH] |Protein Binding/immunology [MESH]The major autoantibody epitope on factor H in atypical hemolytic uremi(epmc).pdf DeepDyve Pubget Overpricing