Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera.

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

Journal

Cell
ISSN: 1097-4172
Titre abrégé: Cell
Pays: United States
ID NLM: 0413066

Informations de publication

Date de publication:
15 04 2021
Historique:
received: 29 01 2021
revised: 06 02 2021
accepted: 13 02 2021
pubmed: 22 3 2021
medline: 29 4 2021
entrez: 21 3 2021
Statut: ppublish

Résumé

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.

Identifiants

DOI: 10.1016/j.cell.2021.02.033 PMID: 33743891 PMC: PMC7891044
pubmed: 33743891
pii: S0092-8674(21)00222-1
doi: 10.1016/j.cell.2021.02.033
pmc: PMC7891044
pii:
doi:

Substances chimiques

Antibodies, Monoclonal 0
Antibodies, Neutralizing 0
Antibodies, Viral 0
Spike Glycoprotein, Coronavirus 0
spike protein, SARS-CoV-2 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2201-2211.e7

Subventions

Organisme : Wellcome Trust
ID : 203224/Z/16/Z
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/V028448/1
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/N00065X/1
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/V001329/1
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/L018942/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 109965/Z/15/Z
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_PC_19055
Pays : United Kingdom

Commentaires et corrections

Type : CommentIn

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests G.R.S. sits on the GSK Vaccines Scientific Advisory Board. Oxford University holds intellectual property related to the Oxford-AstraZeneca vaccine. A.J.P. is Chair of UK Department Health and Social Care’s (DHSC) Joint Committee on Vaccination & Immunisation (JCVI) but does not participate in the JCVI COVID19 committee and is a member of the WHO’s SAGE. S.G. is co-founder of Vaccitech (collaborators in the early development of this vaccine candidate) and named as an inventor on a patent covering use of ChAdOx1-vectored vaccines and a patent application covering this SARS-CoV-2 vaccine. T.L. is named as an inventor on a patent application covering this SARS-CoV-2 vaccine and consultant to Vaccitech. The views expressed in this article do not necessarily represent the views of DHSC, JCVI, or WHO. The University of Oxford has entered into a partnership with AstraZeneca on coronavirus vaccine development. The University of Oxford has protected intellectual property disclosed in this publication.

Références

Science. 2020 Aug 28;369(6507):1119-1123
pubmed: 32661058
Med J Aust. 2020 Jun;212(10):459-462
pubmed: 32237278
Lancet. 2021 Jan 9;397(10269):99-111
pubmed: 33306989
Nat Med. 2021 Apr;27(4):622-625
pubmed: 33654292
Science. 2020 Sep 25;369(6511):1603-1607
pubmed: 32732280
J Mol Biol. 2007 Sep 21;372(3):774-97
pubmed: 17681537
Nat Struct Mol Biol. 2020 Oct;27(10):950-958
pubmed: 32737466
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
pubmed: 15572765
Protein Expr Purif. 2008 Nov;62(1):83-9
pubmed: 18662785
Nat Commun. 2020 Mar 27;11(1):1620
pubmed: 32221306
Acta Crystallogr D Struct Biol. 2018 Feb 1;74(Pt 2):85-97
pubmed: 29533234
Hum Vaccin Immunother. 2020 Dec 1;16(12):2905-2912
pubmed: 33232211
Science. 2021 Jan 8;371(6525):172-177
pubmed: 33172935
PLoS Biol. 2021 Apr 29;19(4):e3001237
pubmed: 33914735
Acta Crystallogr D Biol Crystallogr. 2006 Oct;62(Pt 10):1243-50
pubmed: 17001101
Sci Immunol. 2020 Jul 17;5(49):
pubmed: 32680954
Cell. 2021 Apr 29;184(9):2316-2331.e15
pubmed: 33773105
Immunity. 2020 Aug 18;53(2):248-263
pubmed: 32717182
Antib Ther. 2020 Jul;3(3):205-212
pubmed: 33215063
Science. 2020 Aug 7;369(6504):650-655
pubmed: 32571838
Nature. 2020 Aug;584(7821):450-456
pubmed: 32698192
RNA Biol. 2011 Mar-Apr;8(2):270-9
pubmed: 21593585
Cell Host Microbe. 2021 Mar 10;29(3):463-476.e6
pubmed: 33592168
Cell. 2021 Apr 15;184(8):2183-2200.e22
pubmed: 33756110
Mol Cell. 2020 Dec 17;80(6):1136-1138
pubmed: 33338403
Cell Host Microbe. 2021 May 12;29(5):819-833.e7
pubmed: 33789084
Cell Host Microbe. 2016 Jun 8;19(6):800-13
pubmed: 27281570
J Virol. 2005 Dec;79(23):14614-21
pubmed: 16282461
Vet Q. 2020 Dec;40(1):243-249
pubmed: 32921279
Science. 2020 Aug 21;369(6506):1014-1018
pubmed: 32540904
Cell Host Microbe. 2020 Sep 9;28(3):445-454.e6
pubmed: 32585135
N Engl J Med. 2021 Feb 4;384(5):403-416
pubmed: 33378609
R Soc Open Sci. 2021 Sep 22;8(9):211379
pubmed: 34567593
Cell Rep. 2020 Oct 20;33(3):108274
pubmed: 33027617
Cell. 2020 Sep 3;182(5):1295-1310.e20
pubmed: 32841599
J Mol Biol. 1979 Oct 15;134(1):109-42
pubmed: 537059
Acta Crystallogr D Struct Biol. 2019 Oct 1;75(Pt 10):861-877
pubmed: 31588918
Cell. 2020 Aug 20;182(4):828-842.e16
pubmed: 32645326
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
Cell. 2020 Apr 16;181(2):271-280.e8
pubmed: 32142651
Nature. 2020 May;581(7807):215-220
pubmed: 32225176
N Engl J Med. 2020 Dec 31;383(27):2603-2615
pubmed: 33301246

Auteurs

Piyada Supasa (P)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Daming Zhou (D)

Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.

Wanwisa Dejnirattisai (W)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Chang Liu (C)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK.

Alexander J Mentzer (AJ)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Oxford University Hospitals NHS Foundation Trust, Oxford, UK.

Helen M Ginn (HM)

Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.

Yuguang Zhao (Y)

Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.

Helen M E Duyvesteyn (HME)

Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.

Rungtiwa Nutalai (R)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Aekkachai Tuekprakhon (A)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Beibei Wang (B)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Guido C Paesen (GC)

Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.

Jose Slon-Campos (J)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

César López-Camacho (C)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Bassam Hallis (B)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Naomi Coombes (N)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Kevin R Bewley (KR)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Sue Charlton (S)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Thomas S Walter (TS)

Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.

Eleanor Barnes (E)

Oxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; NIHR Oxford Biomedical Research Centre, Oxford, UK; Translational Gastroenterology Unit, University of Oxford, Oxford, UK.

Susanna J Dunachie (SJ)

Oxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; Centre For Tropical Medicine and Global Health, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Mahidol-Oxford Tropical Medicine Research Unit, Bangkok, Thailand.

Donal Skelly (D)

Oxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; Nuffield Department of Clinical Neurosciences, University of Oxford, Oxford, UK.

Sheila F Lumley (SF)

Oxford University Hospitals NHS Foundation Trust, Oxford, UK; NIHR Oxford Biomedical Research Centre, Oxford, UK; Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Natalie Baker (N)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Imam Shaik (I)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Holly E Humphries (HE)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Kerry Godwin (K)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Nick Gent (N)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Alex Sienkiewicz (A)

National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Christina Dold (C)

NIHR Oxford Biomedical Research Centre, Oxford, UK; Oxford Vaccine Group, Department of Paediatrics, University of Oxford, Oxford, UK.

Robert Levin (R)

Worthing Hospital, Worthing, UK.

Tao Dong (T)

Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Nuffield Department of Medicine, University of Oxford, Oxford, UK; MRC Human Immunology Unit, MRC Weatherall Institute of Molecular Medicine, Radcliffe Department of Medicine, University of Oxford, Oxford, UK.

Andrew J Pollard (AJ)

NIHR Oxford Biomedical Research Centre, Oxford, UK; Oxford Vaccine Group, Department of Paediatrics, University of Oxford, Oxford, UK.

Julian C Knight (JC)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Oxford University Hospitals NHS Foundation Trust, Oxford, UK; NIHR Oxford Biomedical Research Centre, Oxford, UK.

Paul Klenerman (P)

Oxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; NIHR Oxford Biomedical Research Centre, Oxford, UK; Translational Gastroenterology Unit, University of Oxford, Oxford, UK.

Derrick Crook (D)

Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Teresa Lambe (T)

Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Elizabeth Clutterbuck (E)

NIHR Oxford Biomedical Research Centre, Oxford, UK; Oxford Vaccine Group, Department of Paediatrics, University of Oxford, Oxford, UK.

Sagida Bibi (S)

NIHR Oxford Biomedical Research Centre, Oxford, UK; Oxford Vaccine Group, Department of Paediatrics, University of Oxford, Oxford, UK.

Amy Flaxman (A)

Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Mustapha Bittaye (M)

Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Sandra Belij-Rammerstorfer (S)

Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

Sarah Gilbert (S)

Jenner Institute, Nuffield Department of Medicine, University of Oxford, Oxford, UK.

David R Hall (DR)

Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.

Mark A Williams (MA)

Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.

Neil G Paterson (NG)

Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.

William James (W)

Sir William Dunn School of Pathology University of Oxford, Oxford, UK.

Miles W Carroll (MW)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; National Infection Service, Public Health England (PHE), Porton Down, Salisbury, UK.

Elizabeth E Fry (EE)

Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.

Juthathip Mongkolsapaya (J)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Siriraj Center of Research Excellence in Dengue & Emerging Pathogens, Dean Office for Research, Faculty of Medicine Siriraj Hospital, Mahidol University, Thailand. Electronic address: jmongkol@well.ox.ac.uk.

Jingshan Ren (J)

Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK. Electronic address: ren@strubi.ox.ac.uk.

David I Stuart (DI)

Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK; Instruct-ERIC, Oxford House, Parkway Court, John Smith Drive, Oxford, UK. Electronic address: dave@strubi.ox.ac.uk.

Gavin R Screaton (GR)

Wellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK. Electronic address: gavin.screaton@medsci.ox.ac.uk.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Ciara Duggan, Adam L Beckman, Ishani Ganguli et al.
1.00
Humans United States Aged Cross-Sectional Studies Medicare Part C

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Hallie Tankha, Devyn Gaskins, Amanda Shallcross et al.
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Anticorps › Anticorps monoclonaux › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Anticorps › Anticorps neutralisants › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Globulines › Sérum-globulines › Immunoglobulines › Anticorps › Anticorps antiviraux › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules CHO › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Maladies de l'appareil respiratoire › Infections de l'appareil respiratoire › Pneumopathie infectieuse › Pneumopathie virale › COVID-19 › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Cercopithecidae › Cercopithecinae › Cercopithecus › Cercopithecus aethiops › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Arvicolinae › Cricetinae › Cricetulus › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules HEK293 › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Environnement et santé publique › Santé publique › Épidémies de maladies › Épidémies › Pandémies › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Métabolisme › Liaison aux protéines › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Virus › Virus à ARN › Virus à ARN à brin positif › Nidovirales › Coronaviridae › Coronavirus › Betacoronavirus › Virus du SRAS › SARS-CoV-2 › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines virales › Protéines virales structurales › Protéines de l'enveloppe virale › Protéines de fusion virale › Glycoprotéine de spicule des coronavirus › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Phénomènes physiologiques › Phénomènes pharmacologiques et toxicologiques › Phénomènes pharmacologiques › Relation structure-activité › Reduced neutralization of SARS-CoV-2 B.1.1.7...
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules Vero › Reduced neutralization of SARS-CoV-2 B.1.1.7...