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10.1016/j.cell.2020.04.031 http://scihub22266oqcxt.onion/10.1016/j.cell.2020.04.031 32375025!7199733!32375025     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2020 ; 181 (5): 1004-1015.e15 Nephropedia Template TP {{tp|p=32375025|t=2020. Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies |pdf=|usr=}}{{32375025}} gab.com Text Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=32375025 #FOAvip Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks. Twit Text FOAVip Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=32375025 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32375025 #FOAvip English Wikipedia <ref>{{Cite pmid|32375025}}</ref> Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies #MMPMID32375025 Wrapp D; De Vlieger D; Corbett KS; Torres GM; Wang N; Van Breedam W; Roose K; van Schie L; Hoffmann M; Pohlmann S; Graham BS; Callewaert N; Schepens B; Saelens X; McLellan JS Cell 2020[May]; 181 (5): 1004-1015.e15 PMID32375025show ga Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks. |Animals[MESH] |Antibodies, Neutralizing/chemistry/immunology/*isolation & purification[MESH] |Betacoronavirus/*immunology[MESH] |COVID-19[MESH] |Camelids, New World/immunology[MESH] |Coronavirus Infections/therapy[MESH] |Cross Reactions[MESH] |Immunoglobulin G/chemistry/immunology[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Pneumonia, Viral/therapy[MESH] |Protein Domains[MESH] |Receptors, Virus/chemistry[MESH] |SARS-CoV-2[MESH] |Single-Domain Antibodies/chemistry/immunology/*isolation & purification[MESH]Structural Basis for Potent Neutralization of Betacoronaviruses by Sin(epmc).pdf DeepDyve Pubget Overpricing