作者
Daming Zhou, Wanwisa Dejnirattisai, Piyada Supasa, Chang Liu, Alexander J Mentzer, Helen M Ginn, Yuguang Zhao, Helen ME 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
发表日期
2021/4/29
期刊
Cell
卷号
184
期号
9
页码范围
2348-2361. e6
出版商
Cell Press
简介
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 …
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