niman Posted January 14, 2021 Report Share Posted January 14, 2021 (edited) COG-UK has released (at GISAID) a UK Variant B.1.1.7 SARS CoV2 sequences, England/EXET-1405B9/2020, from Exeter, which had acquired Spike E484G. Edited January 14, 2021 by niman Link to comment Share on other sites More sharing options...
niman Posted January 14, 2021 Author Report Share Posted January 14, 2021 England/EXET-1405B9/2020 12/26 matched UK variant with 3 AAs deleted in Spike protein, 3 AAs deleted in NSP6 and Q27 stop codon in NS8. map update https://www.google.com/maps/d/u/1/edit?mid=1aQDSL2LwQFbuoCAg_nIOPK8D-LIJ5MYd&ll=50.7436685025219%2C-3.6669996410059476&z=10 Link to comment Share on other sites More sharing options...
niman Posted January 14, 2021 Author Report Share Posted January 14, 2021 Landscape analysis of escape variants identifies SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization View ORCID ProfileZhuoming Liu, Laura A. VanBlargan, Louis-Marie Bloyet, View ORCID ProfilePaul W. Rothlauf, Rita E. Chen, Spencer Stumpf, Haiyan Zhao, John M. Errico, View ORCID ProfileElitza S. Theel, Mariel J. Liebeskind, Brynn Alford, William J. Buchser, View ORCID ProfileAli H. Ellebedy, View ORCID ProfileDaved H. Fremont, View ORCID ProfileMichael S. Diamond, View ORCID ProfileSean P. J. Whelan doi: https://doi.org/10.1101/2020.11.06.372037 This article is a preprint and has not been certified by peer review [what does this mean?]. Abstract Full Text Info/History Metrics Preview PDF ABSTRACT Although neutralizing antibodies against the SARS-CoV-2 spike (S) protein are a goal of COVID-19 vaccines and have received emergency use authorization as therapeutics, viral escape mutants could compromise their efficacy. To define the immune-selected mutational landscape in S protein, we used a VSV-eGFP-SARS-CoV-2-S chimeric virus and 19 neutralizing monoclonal antibodies (mAbs) against the receptor-binding domain (RBD) to generate 50 different escape mutants. The variants were mapped onto the RBD structure and evaluated for cross-resistance to mAbs and convalescent human sera. Each mAb had a unique resistance profile, although many shared residues within an epitope. Some variants (e.g., S477N) were resistant to neutralization by multiple mAbs, whereas others (e.g., E484K) escaped neutralization by convalescent sera, suggesting some humans induce a narrow repertoire of neutralizing antibodies. Comparing the antibody-mediated mutational landscape in S with sequence variation in circulating SARS-CoV-2, we define substitutions that may attenuate neutralizing immune responses in some humans. https://www.biorxiv.org/content/10.1101/2020.11.06.372037v2.full Link to comment Share on other sites More sharing options...
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