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10.1126/science.abc2241 http://scihub22266oqcxt.onion/10.1126/science.abc2241 32404477!7223722!32404477     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2020 ; 368 (6496): 1274-1278 Nephropedia Template TP {{tp|p=32404477|t=2020. A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2 |pdf=|usr=}}{{32404477}} gab.com Text A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2 JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32404477 #FOAvip Neutralizing antibodies could potentially be used as antivirals against the coronavirus disease 2019 (COVID-19) pandemic. Here, we report isolation of four human-origin monoclonal antibodies from a convalescent patient, all of which display neutralization abilities. The antibodies B38 and H4 block binding between the spike glycoprotein receptor binding domain (RBD) of the virus and the cellular receptor angiotensin-converting enzyme 2 (ACE2). A competition assay indicated different epitopes on the RBD for these two antibodies, making them a potentially promising virus-targeting monoclonal antibody pair for avoiding immune escape in future clinical applications. Moreover, a therapeutic study in a mouse model validated that these antibodies can reduce virus titers in infected lungs. The RBD-B38 complex structure revealed that most residues on the epitope overlap with the RBD-ACE2 binding interface, explaining the blocking effect and neutralizing capacity. Our results highlight the promise of antibody-based therapeutics and provide a structural basis for rational vaccine design. Twit Text FOAVip A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2 ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32404477 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32404477 #FOAvip English Wikipedia <ref>{{Cite pmid|32404477}}</ref> A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2 #MMPMID32404477 Wu Y; Wang F; Shen C; Peng W; Li D; Zhao C; Li Z; Li S; Bi Y; Yang Y; Gong Y; Xiao H; Fan Z; Tan S; Wu G; Tan W; Lu X; Fan C; Wang Q; Liu Y; Zhang C; Qi J; Gao GF; Gao F; Liu L Science 2020[Jun]; 368 (6496): 1274-1278 PMID32404477show ga Neutralizing antibodies could potentially be used as antivirals against the coronavirus disease 2019 (COVID-19) pandemic. Here, we report isolation of four human-origin monoclonal antibodies from a convalescent patient, all of which display neutralization abilities. The antibodies B38 and H4 block binding between the spike glycoprotein receptor binding domain (RBD) of the virus and the cellular receptor angiotensin-converting enzyme 2 (ACE2). A competition assay indicated different epitopes on the RBD for these two antibodies, making them a potentially promising virus-targeting monoclonal antibody pair for avoiding immune escape in future clinical applications. Moreover, a therapeutic study in a mouse model validated that these antibodies can reduce virus titers in infected lungs. The RBD-B38 complex structure revealed that most residues on the epitope overlap with the RBD-ACE2 binding interface, explaining the blocking effect and neutralizing capacity. Our results highlight the promise of antibody-based therapeutics and provide a structural basis for rational vaccine design. |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Antibodies, Monoclonal/immunology/isolation & purification/therapeutic use[MESH] |Antibodies, Neutralizing/immunology/isolation & purification/*therapeutic use[MESH] |Antibodies, Viral/immunology/isolation & purification/*therapeutic use[MESH] |COVID-19[MESH] |Coronavirus Infections/*therapy[MESH] |Disease Models, Animal[MESH] |Humans[MESH] |Immunodominant Epitopes/chemistry/immunology[MESH] |Lung/immunology/virology[MESH] |Mice[MESH] |Neutralization Tests[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/*immunology[MESH] |Pneumonia, Viral/*therapy[MESH] |Protein Domains[MESH] |Receptors, Virus/*immunology[MESH] |Spike Glycoprotein, Coronavirus/*immunology[MESH]A noncompeting pair of human neutralizing antibodies block COVID-19 vi(epmc).pdf DeepDyve Pubget Overpricing