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Title: Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera
Authors: Daming Zhou
Wanwisa Dejnirattisai
Piyada Supasa
Chang Liu
Alexander J. Mentzer
Helen M. Ginn
Yuguang Zhao
Helen M.E. Duyvesteyn
Aekkachai Tuekprakhon
Rungtiwa Nutalai
Beibei Wang
Guido C. Paesen
Cesar Lopez-Camacho
Jose Slon-Campos
Bassam Hallis
Naomi Coombes
Kevin Bewley
Sue Charlton
Thomas S. Walter
Donal Skelly
Sheila F. Lumley
Christina Dold
Robert Levin
Tao Dong
Andrew J. Pollard
Julian C. Knight
Derrick Crook
Teresa Lambe
Elizabeth Clutterbuck
Sagida Bibi
Amy Flaxman
Mustapha Bittaye
Sandra Belij-Rammerstorfer
Sarah Gilbert
William James
Miles W. Carroll
Paul Klenerman
Eleanor Barnes
Susanna J. Dunachie
Elizabeth E. Fry
Juthathip Mongkolsapaya
Jingshan Ren
David I. Stuart
Gavin R. Screaton
Siriraj Hospital
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
Nuffield Department of Medicine
University of Oxford Medical Sciences Division
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 29-Apr-2021
Citation: Cell. Vol.184, No.9 (2021), 2348-2361.e6
Abstract: The race to produce vaccines against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) began when the first sequence was published, and this forms the basis for vaccines currently deployed globally. Independent lineages of SARS-CoV-2 have recently been reported: UK, B.1.1.7; South Africa, B.1.351; and Brazil, P.1. These variants have multiple changes in the immunodominant spike protein that facilitates viral cell entry via the angiotensin-converting enzyme-2 (ACE2) receptor. Mutations in the receptor recognition site on the spike are of great concern for their potential for immune escape. Here, we describe a structure-function analysis of B.1.351 using a large cohort of convalescent and vaccinee serum samples. The receptor-binding domain mutations provide tighter ACE2 binding and widespread escape from monoclonal antibody neutralization largely driven by E484K, although K417N and N501Y act together against some important antibody classes. In a number of cases, it would appear that convalescent and some vaccine serum offers limited protection against this variant.
ISSN: 10974172
Appears in Collections:Scopus 2021

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