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10.1126/science.abc5881 http://scihub22266oqcxt.onion/10.1126/science.abc5881 32703908!7402622!32703908     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       Science 2020 ; 369 (6510): 1505-1509 Nephropedia Template TP {{tp|p=32703908|t=2020. Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody |pdf=|usr=}}{{32703908}} gab.com Text Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32703908 #FOAvip The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in an unprecedented public health crisis. There are no approved vaccines or therapeutics for treating COVID-19. Here we report a humanized monoclonal antibody, H014, that efficiently neutralizes SARS-CoV-2 and SARS-CoV pseudoviruses as well as authentic SARS-CoV-2 at nanomolar concentrations by engaging the spike (S) receptor binding domain (RBD). H014 administration reduced SARS-CoV-2 titers in infected lungs and prevented pulmonary pathology in a human angiotensin-converting enzyme 2 mouse model. Cryo-electron microscopy characterization of the SARS-CoV-2 S trimer in complex with the H014 Fab fragment unveiled a previously uncharacterized conformational epitope, which was only accessible when the RBD was in an open conformation. Biochemical, cellular, virological, and structural studies demonstrated that H014 prevents attachment of SARS-CoV-2 to its host cell receptors. Epitope analysis of available neutralizing antibodies against SARS-CoV and SARS-CoV-2 uncovered broad cross-protective epitopes. Our results highlight a key role for antibody-based therapeutic interventions in the treatment of COVID-19. Twit Text FOAVip Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32703908 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32703908 #FOAvip English Wikipedia <ref>{{Cite pmid|32703908}}</ref> Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody #MMPMID32703908 Lv Z; Deng YQ; Ye Q; Cao L; Sun CY; Fan C; Huang W; Sun S; Sun Y; Zhu L; Chen Q; Wang N; Nie J; Cui Z; Zhu D; Shaw N; Li XF; Li Q; Xie L; Wang Y; Rao Z; Qin CF; Wang X Science 2020[Sep]; 369 (6510): 1505-1509 PMID32703908show ga The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in an unprecedented public health crisis. There are no approved vaccines or therapeutics for treating COVID-19. Here we report a humanized monoclonal antibody, H014, that efficiently neutralizes SARS-CoV-2 and SARS-CoV pseudoviruses as well as authentic SARS-CoV-2 at nanomolar concentrations by engaging the spike (S) receptor binding domain (RBD). H014 administration reduced SARS-CoV-2 titers in infected lungs and prevented pulmonary pathology in a human angiotensin-converting enzyme 2 mouse model. Cryo-electron microscopy characterization of the SARS-CoV-2 S trimer in complex with the H014 Fab fragment unveiled a previously uncharacterized conformational epitope, which was only accessible when the RBD was in an open conformation. Biochemical, cellular, virological, and structural studies demonstrated that H014 prevents attachment of SARS-CoV-2 to its host cell receptors. Epitope analysis of available neutralizing antibodies against SARS-CoV and SARS-CoV-2 uncovered broad cross-protective epitopes. Our results highlight a key role for antibody-based therapeutic interventions in the treatment of COVID-19. |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Antibodies, Monoclonal, Humanized/*chemistry/therapeutic use[MESH] |Antibodies, Neutralizing/*chemistry/therapeutic use[MESH] |Betacoronavirus/*immunology[MESH] |COVID-19[MESH] |Chlorocebus aethiops[MESH] |Coronavirus Infections/therapy[MESH] |Epitope Mapping[MESH] |Humans[MESH] |Immunoglobulin Fab Fragments/chemistry[MESH] |Lung/immunology[MESH] |Mice[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/*immunology[MESH] |Pneumonia, Viral/therapy[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |Receptors, Virus/*immunology[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus/*immunology[MESH]Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a po(epmc).pdf DeepDyve Pubget Overpricing