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10.1038/s41422-021-00487-9 http://scihub22266oqcxt.onion/10.1038/s41422-021-00487-9 33731853!7966918!33731853     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Res 2021 ; 31 (5): 517-525 Nephropedia Template TP {{tp|p=33731853|t=2021. Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies |pdf=|usr=}}{{33731853}} gab.com Text Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies JO: Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=33731853 #FOAvip Neutralizing monoclonal antibodies (nAbs) to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) represent promising candidates for clinical intervention against coronavirus disease 2019 (COVID-19). We isolated a large number of nAbs from SARS-CoV-2-infected individuals capable of disrupting proper interaction between the receptor binding domain (RBD) of the viral spike (S) protein and the receptor angiotensin converting enzyme 2 (ACE2). However, the structural basis for their potent neutralizing activity remains unclear. Here, we report cryo-EM structures of the ten most potent nAbs in their native full-length IgG-form or in both IgG-form and Fab-form bound to the trimeric S protein of SARS-CoV-2. The bivalent binding of the full-length IgG is found to associate with more RBDs in the "up" conformation than the monovalent binding of Fab, perhaps contributing to the enhanced neutralizing activity of IgG and triggering more shedding of the S1 subunit from the S protein. Comparison of a large number of nAbs identified common and unique structural features associated with their potent neutralizing activities. This work provides a structural basis for further understanding the mechanism of nAbs, especially through revealing the bivalent binding and its correlation with more potent neutralization and the shedding of S1 subunit. Twit Text FOAVip Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies ????Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=33731853 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33731853 #FOAvip English Wikipedia <ref>{{Cite pmid|33731853}}</ref> Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies #MMPMID33731853 Yan R; Wang R; Ju B; Yu J; Zhang Y; Liu N; Wang J; Zhang Q; Chen P; Zhou B; Li Y; Shen Y; Zhang S; Tian L; Guo Y; Xia L; Zhong X; Cheng L; Ge X; Zhao J; Wang HW; Wang X; Zhang Z; Zhang L; Zhou Q Cell Res 2021[May]; 31 (5): 517-525 PMID33731853show ga Neutralizing monoclonal antibodies (nAbs) to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) represent promising candidates for clinical intervention against coronavirus disease 2019 (COVID-19). We isolated a large number of nAbs from SARS-CoV-2-infected individuals capable of disrupting proper interaction between the receptor binding domain (RBD) of the viral spike (S) protein and the receptor angiotensin converting enzyme 2 (ACE2). However, the structural basis for their potent neutralizing activity remains unclear. Here, we report cryo-EM structures of the ten most potent nAbs in their native full-length IgG-form or in both IgG-form and Fab-form bound to the trimeric S protein of SARS-CoV-2. The bivalent binding of the full-length IgG is found to associate with more RBDs in the "up" conformation than the monovalent binding of Fab, perhaps contributing to the enhanced neutralizing activity of IgG and triggering more shedding of the S1 subunit from the S protein. Comparison of a large number of nAbs identified common and unique structural features associated with their potent neutralizing activities. This work provides a structural basis for further understanding the mechanism of nAbs, especially through revealing the bivalent binding and its correlation with more potent neutralization and the shedding of S1 subunit. |Angiotensin-Converting Enzyme 2/immunology[MESH] |Antibodies, Neutralizing/chemistry/*immunology/ultrastructure[MESH] |Antibodies, Viral/chemistry/immunology/ultrastructure[MESH] |COVID-19/*immunology[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Immunoglobulin G/chemistry/*immunology/ultrastructure[MESH] |Models, Molecular[MESH] |Protein Conformation[MESH] |Protein Multimerization[MESH] |SARS-CoV-2/*immunology/physiology[MESH]Structural basis for bivalent binding and inhibition of SARS-CoV-2 inf(epmc).pdf DeepDyve Pubget Overpricing