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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.

Original publication

DOI

10.1016/j.cell.2021.02.037

Type

Journal article

Journal

Cell

Publication Date

29/04/2021

Volume

184

Pages

2348 - 2361.e6

Keywords

ACE2, B.1.351, SARS-CoV-2, South Africa, antibody, escape, neutralization, receptor-binding domain, vaccine, variant, Animals, Antibodies, Monoclonal, COVID-19, COVID-19 Vaccines, Chlorocebus aethiops, Clinical Trials as Topic, HEK293 Cells, Humans, Immunization, Passive, Models, Molecular, Mutation, Neutralization Tests, Protein Binding, SARS-CoV-2, Vero Cells