Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera
| Autor: | Derrick W. Crook, Eleanor Barnes, Naomi Coombes, D. Zhou, Jingshan Ren, Duyvesteyn Hme., Bassam Hallis, Alexander J. Mentzer, Christina Dold, Sheila F Lumley, Cesar Lopez-Camacho, Aekkachai Tuekprakhon, Elizabeth E. Fry, Guido C. Paesen, Thomas S. Walter, Donal T. Skelly, Beibei Wang, Helen M. Ginn, David I. Stuart, Chang Liu, Sandra Belij-Rammerstorfer, Julian C. Knight, Susanna Dunachie, Juthathip Mongkolsapaya, S Bibi, Teresa Lambe, Amy Flaxman, Sarah C. Gilbert, P Supasa, Wanwisa Dejnirattisai, Paul Klenerman, M Bittaye, Miles W. Carroll, Tao Dong, Sue Charlton, R Levin, R Nutalai, Yuguang Zhao, William James, Gavin R. Screaton, Kevin R. Bewley, Elizabeth A. Clutterbuck, J Slon-Campos, Andrew J. Pollard |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular COVID-19 Vaccines medicine.drug_class Plasma protein binding Biology Monoclonal antibody medicine.disease_cause Article General Biochemistry Genetics and Molecular Biology Neutralization 03 medical and health sciences 0302 clinical medicine Neutralization Tests Chlorocebus aethiops medicine Animals Humans Receptor Vero Cells COVID-19 Serotherapy 030304 developmental biology 0303 health sciences Mutation Clinical Trials as Topic SARS-CoV-2 HEK 293 cells Immunization Passive Antibodies Monoclonal COVID-19 Virology HEK293 Cells biology.protein Vero cell Antibody 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Cell |
| ISSN: | 1097-4172 |
| Popis: | The race to produce vaccines against 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 which 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. Structure-function analysis of the SARS-CoV-2 variant B.1.351 using serum samples from convalescent and vaccinated individuals reveals how mutations in the viral spike protein result in tighter binding to the receptor ACE2 and allow escape from monoclonal antibody neutralization. |
| Databáze: | OpenAIRE |
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