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10.1038/s41467-020-20465-w http://scihub22266oqcxt.onion/10.1038/s41467-020-20465-w 33431876!7801428!33431876     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       Nat+Commun 2021 ; 12 (1): 264 Nephropedia Template TP {{tp|p=33431876|t=2021. Development and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections |pdf=|usr=}}{{33431876}} gab.com Text Development and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33431876 #FOAvip The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 A resolution, revealing the conformational space of the antigen-antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections. Twit Text FOAVip Development and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33431876 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33431876 #FOAvip English Wikipedia <ref>{{Cite pmid|33431876}}</ref> Development and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections #MMPMID33431876 Zhang C; Wang Y; Zhu Y; Liu C; Gu C; Xu S; Wang Y; Zhou Y; Wang Y; Han W; Hong X; Yang Y; Zhang X; Wang T; Xu C; Hong Q; Wang S; Zhao Q; Qiao W; Zang J; Kong L; Wang F; Wang H; Qu D; Lavillette D; Tang H; Deng Q; Xie Y; Cong Y; Huang Z Nat Commun 2021[Jan]; 12 (1): 264 PMID33431876show ga The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 A resolution, revealing the conformational space of the antigen-antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections. |*COVID-19 Drug Treatment[MESH] |Animals[MESH] |Antibodies, Monoclonal/*chemistry/immunology/*pharmacology/therapeutic use[MESH] |Antibodies, Neutralizing/immunology[MESH] |Antibodies, Viral/*chemistry/immunology/*pharmacology/therapeutic use[MESH] |Cryoelectron Microscopy[MESH] |Epitope Mapping[MESH] |Epitopes[MESH] |Female[MESH] |Mice[MESH] |Mice, Inbred BALB C[MESH] |Models, Molecular[MESH] |Protein Binding/drug effects[MESH] |Protein Conformation[MESH] |SARS-CoV-2/*drug effects[MESH]Development and structural basis of a two-MAb cocktail for treating SA(epmc).pdf DeepDyve Pubget Overpricing