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10.1126/science.abh1139 http://scihub22266oqcxt.onion/10.1126/science.abh1139 34016740!8284396!34016740     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2021 ; 373 (6556): 818-823 Nephropedia Template TP {{tp|p=34016740|t=2021. Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants |pdf=|usr=}}{{34016740}} gab.com Text Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=34016740 #FOAvip Neutralizing antibodies (nAbs) elicited against the receptor binding site (RBS) of the spike protein of wild-type severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are generally less effective against recent variants of concern. RBS residues Glu(484), Lys(417), and Asn(501) are mutated in variants first described in South Africa (B.1.351) and Brazil (P.1). We analyzed their effects on angiotensin-converting enzyme 2 binding, as well as the effects of two of these mutations (K417N and E484K) on nAbs isolated from COVID-19 patients. Binding and neutralization of the two most frequently elicited antibody families (IGHV3-53/3-66 and IGHV1-2), which can both bind the RBS in alternative binding modes, are abrogated by K417N, E484K, or both. These effects can be structurally explained by their extensive interactions with RBS nAbs. However, nAbs to the more conserved, cross-neutralizing CR3022 and S309 sites were largely unaffected. The results have implications for next-generation vaccines and antibody therapies. Twit Text FOAVip Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants ????Science http://www.kidney.de/pget.php?&tw=1&pmid=34016740 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34016740 #FOAvip English Wikipedia <ref>{{Cite pmid|34016740}}</ref> Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants #MMPMID34016740 Yuan M; Huang D; Lee CD; Wu NC; Jackson AM; Zhu X; Liu H; Peng L; van Gils MJ; Sanders RW; Burton DR; Reincke SM; Pruss H; Kreye J; Nemazee D; Ward AB; Wilson IA Science 2021[Aug]; 373 (6556): 818-823 PMID34016740show ga Neutralizing antibodies (nAbs) elicited against the receptor binding site (RBS) of the spike protein of wild-type severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are generally less effective against recent variants of concern. RBS residues Glu(484), Lys(417), and Asn(501) are mutated in variants first described in South Africa (B.1.351) and Brazil (P.1). We analyzed their effects on angiotensin-converting enzyme 2 binding, as well as the effects of two of these mutations (K417N and E484K) on nAbs isolated from COVID-19 patients. Binding and neutralization of the two most frequently elicited antibody families (IGHV3-53/3-66 and IGHV1-2), which can both bind the RBS in alternative binding modes, are abrogated by K417N, E484K, or both. These effects can be structurally explained by their extensive interactions with RBS nAbs. However, nAbs to the more conserved, cross-neutralizing CR3022 and S309 sites were largely unaffected. The results have implications for next-generation vaccines and antibody therapies. |Angiotensin-Converting Enzyme 2/metabolism[MESH] |Antibodies, Neutralizing/*immunology/metabolism[MESH] |Antibodies, Viral/*immunology/metabolism[MESH] |Antigenic Variation[MESH] |Antigens, Viral/chemistry/genetics/*immunology/metabolism[MESH] |Binding Sites[MESH] |Binding Sites, Antibody[MESH] |COVID-19/*immunology/virology[MESH] |Epitopes[MESH] |Humans[MESH] |Immune Evasion[MESH] |Mutation[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Receptors, Coronavirus/metabolism[MESH] |SARS-CoV-2/chemistry/genetics/*immunology[MESH]Structural and functional ramifications of antigenic drift in recent S(epmc).pdf DeepDyve Pubget Overpricing