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10.1038/s41589-020-00679-1 http://scihub22266oqcxt.onion/10.1038/s41589-020-00679-1 33082574!8356808!33082574     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       Nat+Chem+Biol 2021 ; 17 (1): 113-121 Nephropedia Template TP {{tp|p=33082574|t=2021. Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2 |pdf=|usr=}}{{33082574}} gab.com Text Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2 JO: Nat Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=33082574 #FOAvip Neutralizing agents against SARS-CoV-2 are urgently needed for the treatment and prophylaxis of COVID-19. Here, we present a strategy to rapidly identify and assemble synthetic human variable heavy (VH) domains toward neutralizing epitopes. We constructed a VH-phage library and targeted the angiotensin-converting enzyme 2 (ACE2) binding interface of the SARS-CoV-2 Spike receptor-binding domain (Spike-RBD). Using a masked selection approach, we identified VH binders to two non-overlapping epitopes and further assembled these into multivalent and bi-paratopic formats. These VH constructs showed increased affinity to Spike (up to 600-fold) and neutralization potency (up to 1,400-fold) on pseudotyped SARS-CoV-2 virus when compared to standalone VH domains. The most potent binder, a trivalent VH, neutralized authentic SARS-CoV-2 with a half-maximal inhibitory concentration (IC(50)) of 4.0 nM (180 ng ml(-1)). A cryo-EM structure of the trivalent VH bound to Spike shows each VH domain engaging an RBD at the ACE2 binding site, confirming our original design strategy. Twit Text FOAVip Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2 ????Nat Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=33082574 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33082574 #FOAvip English Wikipedia <ref>{{Cite pmid|33082574}}</ref> Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2 #MMPMID33082574 Bracken CJ; Lim SA; Solomon P; Rettko NJ; Nguyen DP; Zha BS; Schaefer K; Byrnes JR; Zhou J; Lui I; Liu J; Pance K; Zhou XX; Leung KK; Wells JA Nat Chem Biol 2021[Jan]; 17 (1): 113-121 PMID33082574show ga Neutralizing agents against SARS-CoV-2 are urgently needed for the treatment and prophylaxis of COVID-19. Here, we present a strategy to rapidly identify and assemble synthetic human variable heavy (VH) domains toward neutralizing epitopes. We constructed a VH-phage library and targeted the angiotensin-converting enzyme 2 (ACE2) binding interface of the SARS-CoV-2 Spike receptor-binding domain (Spike-RBD). Using a masked selection approach, we identified VH binders to two non-overlapping epitopes and further assembled these into multivalent and bi-paratopic formats. These VH constructs showed increased affinity to Spike (up to 600-fold) and neutralization potency (up to 1,400-fold) on pseudotyped SARS-CoV-2 virus when compared to standalone VH domains. The most potent binder, a trivalent VH, neutralized authentic SARS-CoV-2 with a half-maximal inhibitory concentration (IC(50)) of 4.0 nM (180 ng ml(-1)). A cryo-EM structure of the trivalent VH bound to Spike shows each VH domain engaging an RBD at the ACE2 binding site, confirming our original design strategy. |Angiotensin-Converting Enzyme 2/antagonists & inhibitors/*chemistry/genetics/immunology[MESH] |Animals[MESH] |Antibodies, Neutralizing/*chemistry/genetics/immunology[MESH] |Antibodies, Viral/*chemistry/genetics/immunology[MESH] |Binding Sites, Antibody/genetics/immunology[MESH] |Chlorocebus aethiops[MESH] |Cryoelectron Microscopy[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Models, Molecular[MESH] |Peptide Library[MESH] |Protein Binding[MESH] |Protein Conformation, alpha-Helical[MESH] |Protein Conformation, beta-Strand[MESH] |Protein Interaction Domains and Motifs[MESH] |SARS-CoV-2[MESH] |Single-Chain Antibodies/*chemistry/genetics/immunology[MESH] |Spike Glycoprotein, Coronavirus/antagonists & inhibitors/*chemistry/genetics/immunology[MESH]Bi-paratopic and multivalent VH domains block ACE2 binding and neutral(epmc).pdf DeepDyve Pubget Overpricing