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10.1016/j.chom.2020.04.023 http://scihub22266oqcxt.onion/10.1016/j.chom.2020.04.023 32413276!7224157!32413276     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       Cell+Host+Microbe 2020 ; 27 (6): 891-898.e5 Nephropedia Template TP {{tp|p=32413276|t=2020. Identification of Human Single-Domain Antibodies against SARS-CoV-2 |pdf=|usr=}}{{32413276}} gab.com Text Identification of Human Single-Domain Antibodies against SARS-CoV-2 JO: Cell Host Microbe http://www.kidney.de/pget.php?&tw=1&pmid=32413276 #FOAvip The worldwide spread of COVID-19 highlights the need for an efficient approach to rapidly develop therapeutics and prophylactics against SARS-CoV-2. The SARS-CoV-2 spike protein, containing the receptor-binding domain (RBD) and S1 subunit involved in receptor engagement, is a potential therapeutic target. We describe the development of a phage-displayed single-domain antibody library by grafting naive complementarity-determining regions (CDRs) into framework regions of a human germline immunoglobulin heavy chain variable region (IGHV) allele. Panning this library against SARS-CoV-2 RBD and S1 subunit identified fully human single-domain antibodies targeting five distinct epitopes on SARS-CoV-2 RBD with subnanomolar to low nanomolar affinities. Some of these antibodies neutralize SARS-CoV-2 by targeting a cryptic epitope located in the spike trimeric interface. Collectively, this work presents a versatile platform for rapid antibody isolation and identifies promising therapeutic anti-SARS-CoV-2 antibodies as well as the diverse immogneic profile of the spike protein. Twit Text FOAVip Identification of Human Single-Domain Antibodies against SARS-CoV-2 ????Cell Host Microbe http://www.kidney.de/pget.php?&tw=1&pmid=32413276 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32413276 #FOAvip English Wikipedia <ref>{{Cite pmid|32413276}}</ref> Identification of Human Single-Domain Antibodies against SARS-CoV-2 #MMPMID32413276 Wu Y; Li C; Xia S; Tian X; Kong Y; Wang Z; Gu C; Zhang R; Tu C; Xie Y; Yang Z; Lu L; Jiang S; Ying T Cell Host Microbe 2020[Jun]; 27 (6): 891-898.e5 PMID32413276show ga The worldwide spread of COVID-19 highlights the need for an efficient approach to rapidly develop therapeutics and prophylactics against SARS-CoV-2. The SARS-CoV-2 spike protein, containing the receptor-binding domain (RBD) and S1 subunit involved in receptor engagement, is a potential therapeutic target. We describe the development of a phage-displayed single-domain antibody library by grafting naive complementarity-determining regions (CDRs) into framework regions of a human germline immunoglobulin heavy chain variable region (IGHV) allele. Panning this library against SARS-CoV-2 RBD and S1 subunit identified fully human single-domain antibodies targeting five distinct epitopes on SARS-CoV-2 RBD with subnanomolar to low nanomolar affinities. Some of these antibodies neutralize SARS-CoV-2 by targeting a cryptic epitope located in the spike trimeric interface. Collectively, this work presents a versatile platform for rapid antibody isolation and identifies promising therapeutic anti-SARS-CoV-2 antibodies as well as the diverse immogneic profile of the spike protein. |*Peptide Library[MESH] |Antibodies, Monoclonal/chemistry/immunology[MESH] |Antibodies, Neutralizing/immunology[MESH] |Epitopes/immunology[MESH] |Humans[MESH] |Immunoglobulin Heavy Chains[MESH] |Immunoglobulin Variable Region[MESH] |Models, Molecular[MESH] |Protein Domains[MESH] |Single-Domain Antibodies/chemistry/immunology/*isolation & purification[MESH]Identification of Human Single-Domain Antibodies against SARS-CoV-2 (epmc).pdf DeepDyve Pubget Overpricing