Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera | Zendy

Daming Zhou | Zendy; Wanwisa Dejnirattisai | Zendy; Piyada Supasa | Zendy; Chang Liu | Zendy; Alexander J. Mentzer | Zendy; Helen M. Ginn | Zendy; Yuguang Zhao | Zendy; Helen M. E. Duyvesteyn | Zendy; Aekkachai Tuekprakhon | Zendy; Rungtiwa Nutalai | Zendy; Beibei Wang | Zendy; Guido C. Paesen | Zendy; César LópezCamacho | Zendy; Jose Slon-Campos | Zendy; Bassam Hallis | Zendy; Naomi S. Coombes | Zendy; Kevin R. Bewley | Zendy; Sue Charlton | Zendy; Thomas S. Walter | Zendy; Donal Skelly | Zendy; Sheila Lumley | Zendy; Christina Dold | Zendy; Robert H. Levin | Zendy; Tao Dong | Zendy; Andrew J. Pollard | Zendy; Julian C. Knight | Zendy; Derrick W. Crook | Zendy; Teresa Lambe | Zendy; Elizabeth Clutterbuck | Zendy; Sagida Bibi | Zendy; Amy Flaxman | Zendy; Mustapha Bittaye | Zendy; Sandra BelijRammerstorfer | Zendy; Sarah C. Gilbert | Zendy; William James | Zendy; Miles W. Carroll | Zendy; Paul Klenerman | Zendy; Eleanor Barnes | Zendy; Susanna Dunachie | Zendy; Elizabeth E. Fry | Zendy; Juthathip Mongkolsapaya | Zendy; Jingshan Ren | Zendy; David I. Stuart | Zendy; Gavin Screaton | Zendy

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Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera

Author(s) -

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,

César LópezCamacho,

Jose Slon-Campos,

Bassam Hallis,

Naomi S. Coombes,

Kevin R. Bewley,

Sue Charlton,

Thomas S. Walter,

Donal Skelly,

Sheila Lumley,

Christina Dold,

Robert H. Levin,

Tao Dong,

Andrew J. Pollard,

Julian C. Knight,

Derrick W. Crook,

Teresa Lambe,

Elizabeth Clutterbuck,

Sagida Bibi,

Amy Flaxman,

Mustapha Bittaye,

Sandra BelijRammerstorfer,

Sarah C. Gilbert,

William James,

Miles W. Carroll,

Paul Klenerman,

Eleanor Barnes,

Susanna Dunachie,

Elizabeth E. Fry,

Juthathip Mongkolsapaya,

Jingshan Ren,

David I. Stuart,

Gavin Screaton

Publication year - 2021

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2021.02.037

Subject(s) - biology , virology , spike protein , antibody , neutralization , covid-19 , receptor , coronavirus , immunology , betacoronavirus , monoclonal antibody , neutralizing antibody , genetics , disease , medicine , pathology , infectious disease (medical specialty)

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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