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10.1080/19420862.2021.1893426 http://scihub22266oqcxt.onion/10.1080/19420862.2021.1893426 33666135!7939556!33666135     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33666135&cmd=llinks): Failed to open stream: HTTP request failed! 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Bispecific VH/Fab antibodies targeting neutralizing and non-neutralizing Spike epitopes demonstrate enhanced potency against SARS-CoV-2 |pdf=|usr=}}{{33666135}} gab.com Text Bispecific VH/Fab antibodies targeting neutralizing and non-neutralizing Spike epitopes demonstrate enhanced potency against SARS-CoV-2 JO: MAbs http://www.kidney.de/pget.php?&tw=1&pmid=33666135 #FOAvip Numerous neutralizing antibodies that target SARS-CoV-2 have been reported, and most directly block binding of the viral Spike receptor-binding domain (RBD) to angiotensin-converting enzyme II (ACE2). Here, we deliberately exploit non-neutralizing RBD antibodies, showing they can dramatically assist in neutralization when linked to neutralizing binders. We identified antigen-binding fragments (Fabs) by phage display that bind RBD, but do not block ACE2 or neutralize virus as IgGs. When these non-neutralizing Fabs were assembled into bispecific VH/Fab IgGs with a neutralizing VH domain, we observed a ~ 25-fold potency improvement in neutralizing SARS-CoV-2 compared to the mono-specific bi-valent VH-Fc alone or the cocktail of the VH-Fc and IgG. This effect was epitope-dependent, reflecting the unique geometry of the bispecific antibody toward Spike. Our results show that a bispecific antibody that combines both neutralizing and non-neutralizing epitopes on Spike-RBD is a promising and rapid engineering strategy to improve the potency of SARS-CoV-2 antibodies. Twit Text FOAVip Bispecific VH/Fab antibodies targeting neutralizing and non-neutralizing Spike epitopes demonstrate enhanced potency against SARS-CoV-2 ????MAbs http://www.kidney.de/pget.php?&tw=1&pmid=33666135 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33666135 #FOAvip English Wikipedia <ref>{{Cite pmid|33666135}}</ref> Bispecific VH/Fab antibodies targeting neutralizing and non-neutralizing Spike epitopes demonstrate enhanced potency against SARS-CoV-2 #MMPMID33666135 Lim SA; Gramespacher JA; Pance K; Rettko NJ; Solomon P; Jin J; Lui I; Elledge SK; Liu J; Bracken CJ; Simmons G; Zhou XX; Leung KK; Wells JA MAbs 2021[Jan]; 13 (1): 1893426 PMID33666135show ga Numerous neutralizing antibodies that target SARS-CoV-2 have been reported, and most directly block binding of the viral Spike receptor-binding domain (RBD) to angiotensin-converting enzyme II (ACE2). Here, we deliberately exploit non-neutralizing RBD antibodies, showing they can dramatically assist in neutralization when linked to neutralizing binders. We identified antigen-binding fragments (Fabs) by phage display that bind RBD, but do not block ACE2 or neutralize virus as IgGs. When these non-neutralizing Fabs were assembled into bispecific VH/Fab IgGs with a neutralizing VH domain, we observed a ~ 25-fold potency improvement in neutralizing SARS-CoV-2 compared to the mono-specific bi-valent VH-Fc alone or the cocktail of the VH-Fc and IgG. This effect was epitope-dependent, reflecting the unique geometry of the bispecific antibody toward Spike. Our results show that a bispecific antibody that combines both neutralizing and non-neutralizing epitopes on Spike-RBD is a promising and rapid engineering strategy to improve the potency of SARS-CoV-2 antibodies. |Antibodies, Bispecific/genetics/*immunology/therapeutic use[MESH] |Antibodies, Neutralizing/genetics/*immunology/therapeutic use[MESH] |Antibodies, Viral/genetics/*immunology/therapeutic use[MESH] |COVID-19 Drug Treatment[MESH] |COVID-19/genetics/*immunology[MESH] |Epitopes/genetics/*immunology[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Immunoglobulin Fab Fragments/genetics/*immunology/therapeutic use[MESH] |SARS-CoV-2/genetics/*immunology[MESH]Bispecific VH/Fab antibodies targeting neutralizing and non-neutralizi(epmc).pdf DeepDyve Pubget Overpricing