Journal
CELL
Volume 184, Issue 9, Pages 2348-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2021.02.037
Keywords
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Categories
Funding
- Chinese Academy of Medical Sciences (CAMS) Innovation Fund for Medical Science (CIFMS), China [2018-I2M-2-002]
- Wellcome Trust [101122/Z/13/Z, 095541/A/11/Z, 090532/Z/09/Z, 203141/Z/16/Z]
- Cancer Research UK [C375/A17721]
- UK Medical Research Council [MR/N00065X/1]
- FastGrants, Mercatus Center
- NIHR Oxford BRC
- UK Research and Innovation, Coalition for Epidemic Preparedness Innovations
- National Institute for Health Research (NIHR)
- NIHR Oxford Biomedical Research Centre
- Thames Valley and South Midland's NIHR Clinical Research Network
- UK Department of Health and Social Care as part of the PITCH (Protective Immunity from T cells to COVID-19 in Health Workers) Consortium
- UK Coronavirus Immunology Consortium (UK-CIC)
- Huo Family Foundation
- NIH [U19 I082360]
- CIFMS
- Wellcome Trust
- [WT109965MA]
- MRC [MR/L018942/1] Funding Source: UKRI
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The race to develop vaccines against SARS-CoV-2 variants, such as B.1.1.7, B.1.351, and P.1, is ongoing as these variants have mutations in the spike protein, potentially leading to immune escape. A structure-function analysis of B.1.351 revealed tighter ACE2 binding and widespread evasion from monoclonal antibody neutralization, particularly driven by the E484K mutation.
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.
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