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SARS-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.

Original publication

DOI

10.1016/j.cell.2021.02.033

Type

Journal article

Journal

Cell

Publication Date

15/04/2021

Volume

184

Pages

2201 - 2211.e7

Keywords

B.1.1.7, IGHV3-53, Kent, SARS-CoV-2, antibody, escape, neutralization, variant, Animals, Antibodies, Monoclonal, Antibodies, Neutralizing, Antibodies, Viral, CHO Cells, COVID-19, Chlorocebus aethiops, Cricetulus, HEK293 Cells, Humans, Pandemics, Protein Binding, SARS-CoV-2, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Vero Cells