Browsing by Author "Nick Gent"
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Publication Metadata only Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera(2021-04-15) Piyada Supasa; Daming Zhou; Wanwisa Dejnirattisai; Chang Liu; Alexander J. Mentzer; Helen M. Ginn; Yuguang Zhao; Helen M.E. Duyvesteyn; Rungtiwa Nutalai; Aekkachai Tuekprakhon; Beibei Wang; Guido C. Paesen; Jose Slon-Campos; César López-Camacho; Bassam Hallis; Naomi Coombes; Kevin R. Bewley; Sue Charlton; Thomas S. Walter; Eleanor Barnes; Susanna J. Dunachie; Donal Skelly; Sheila F. Lumley; Natalie Baker; Imam Shaik; Holly E. Humphries; Kerry Godwin; Nick Gent; Alex Sienkiewicz; Christina Dold; Robert Levin; Tao Dong; Andrew J. Pollard; Julian C. Knight; Paul Klenerman; Derrick Crook; Teresa Lambe; Elizabeth Clutterbuck; Sagida Bibi; Amy Flaxman; Mustapha Bittaye; Sandra Belij-Rammerstorfer; Sarah Gilbert; David R. Hall; Mark A. Williams; Neil G. Paterson; William James; Miles W. Carroll; Elizabeth E. Fry; Juthathip Mongkolsapaya; Jingshan Ren; David I. Stuart; Gavin R. Screaton; Mahidol Oxford Tropical Medicine Research Unit; NIHR Oxford Biomedical Research Centre; Oxford University Hospitals NHS Foundation Trust; Public Health England; Diamond Light Source; Worthing Hospital; University of Oxford; Sir William Dunn School of Pathology; Faculty of Medicine Siriraj Hospital, Mahidol University; Nuffield Department of Medicine; University of Oxford Medical Sciences Division; Instruct-ERICSARS-CoV-2 has caused over 2 million deaths in little over a year. Vaccines are being deployed at scale, aiming to generate responses against the virus spike. The scale of the pandemic and error-prone virus replication is leading to the appearance of mutant viruses and potentially escape from antibody responses. Variant B.1.1.7, now dominant in the UK, with increased transmission, harbors 9 amino acid changes in the spike, including N501Y in the ACE2 interacting surface. We examine the ability of B.1.1.7 to evade antibody responses elicited by natural SARS-CoV-2 infection or vaccination. We map the impact of N501Y by structure/function analysis of a large panel of well-characterized monoclonal antibodies. B.1.1.7 is harder to neutralize than parental virus, compromising neutralization by some members of a major class of public antibodies through light-chain contacts with residue 501. However, widespread escape from monoclonal antibodies or antibody responses generated by natural infection or vaccination was not observed.
