Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma.
Animals
Antibodies, Neutralizing
/ biosynthesis
Antibodies, Viral
/ biosynthesis
COVID-19
/ epidemiology
Cell Line
Chlorocebus aethiops
Humans
Immune Evasion
/ genetics
Immunization, Passive
Mutation
Neutralization Tests
SARS-CoV-2
/ genetics
South Africa
/ epidemiology
Time Factors
Vero Cells
COVID-19 Serotherapy
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
05 2021
05 2021
Historique:
received:
21
01
2021
accepted:
18
03
2021
pubmed:
30
3
2021
medline:
12
5
2021
entrez:
29
3
2021
Statut:
ppublish
Résumé
SARS-CoV-2 variants of concern (VOC) have arisen independently at multiple locations
Identifiants
pubmed: 33780970
doi: 10.1038/s41586-021-03471-w
pii: 10.1038/s41586-021-03471-w
pmc: PMC9867906
mid: NIHMS1863674
doi:
Substances chimiques
Antibodies, Neutralizing
0
Antibodies, Viral
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
142-146Subventions
Organisme : NIDA NIH HHS
ID : DP2 DA040254
Pays : United States
Investigateurs
Shareef Abrahams
(S)
Luiz Carlos Junior Alcantara
(LCJ)
Arghavan Alisoltani-Dehkordi
(A)
Mushal Allam
(M)
Jinal N Bhiman
(JN)
Mary-Ann Davies
(MA)
Deelan Doolabh
(D)
Susan Engelbrecht
(S)
Vagner Fonseca
(V)
Marta Giovanetti
(M)
Allison J Glass
(AJ)
Adam Godzik
(A)
Dominique Goedhals
(D)
Diana Hardie
(D)
Marvin Hsiao
(M)
Arash Iranzadeh
(A)
Arshad Ismail
(A)
Stephen Korsman
(S)
Sergei L Kosakovsky Pond
(SLK)
Oluwakemi Laguda-Akingba
(O)
Jose Lourenco
(J)
Gert Marais
(G)
Darren Martin
(D)
Caroline Maslo
(C)
Koleka Mlisana
(K)
Thabo Mohale
(T)
Nokukhanya Msomi
(N)
Innocent Mudau
(I)
Francesco Petruccione
(F)
Wolfgang Preiser
(W)
Emmanuel James San
(EJ)
Bryan Trevor Sewell
(BT)
Lynn Tyers
(L)
Gert Van Zyl
(G)
Anne von Gottberg
(A)
Sibongile Walaza
(S)
Steven Weaver
(S)
Constantinos Kurt Wibmer
(CK)
Carolyn Williamson
(C)
Denis York
(D)
Moherndran Archary
(M)
Kaylesh J Dullabh
(KJ)
Philip Goulder
(P)
Sashin Harilall
(S)
Guy Harling
(G)
Rohen Harrichandparsad
(R)
Kobus Herbst
(K)
Prakash Jeena
(P)
Thandeka Khoza
(T)
Nigel Klein
(N)
Henrik Kløverpris
(H)
Alasdair Leslie
(A)
Rajhmun Madansein
(R)
Mohlopheni Marakalala
(M)
Matilda Mazibuko
(M)
Mosa Moshabela
(M)
Ntombifuthi Mthabela
(N)
Kogie Naidoo
(K)
Zaza Ndhlovu
(Z)
Thumbi Ndung'u
(T)
Kennedy Nyamande
(K)
Nesri Padayatchi
(N)
Vinod Patel
(V)
Dirhona Ramjit
(D)
Hylton Rodel
(H)
Theresa Smit
(T)
Adrie Steyn
(A)
Emily Wong
(E)
Références
Tegally, H. et al. Detection of a SARS-CoV-2 variant of concern in South Africa. Nature https://doi.org/10.1038/s41586-021-03402-9 (2021).
doi: 10.1038/s41586-021-03402-9
Faria, N. R. et al. Genomics and epidemiology of a novel SARS-CoV-2 lineage in Manaus, Brazil. Preprint at https://doi.org/10.1101/2021.02.26.21252554 (2021).
Madhi, S. A. et al. Efficacy of the ChAdOx1 nCoV-19 COVID-19 vaccine against the B.1.351 variant. N. Engl. J. Med. https://doi.org/10.1056/NEJMoa2102214 (2021).
doi: 10.1056/NEJMoa2102214
pubmed: 33725432
pmcid: 7993410
Piccoli, L. et al. Mapping neutralizing and immunodominant sites on the SARS-CoV-2 spike receptor-binding domain by structure-guided high-resolution serology. Cell 183, 1024–1042 (2020).
doi: 10.1016/j.cell.2020.09.037
McCallum, M. et al. N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2. Cell https://doi.org/10.1016/j.cell.2021.03.028 (2021).
Barnes, C. O. et al. SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies. Nature 588, 682–687 (2020).
doi: 10.1038/s41586-020-2852-1
Baum, A. et al. Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies. Science 369, 1014–1018 (2020).
doi: 10.1126/science.abd0831
Greaney, A. J. et al. Complete mapping of mutations to the SARS-CoV-2 spike receptor-binding domain that escape antibody recognition. Cell Host Microbe 29, 44–57 (2021).
doi: 10.1016/j.chom.2020.11.007
Weisblum, Y. et al. Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants. eLife 9, e61312 (2020).
doi: 10.7554/eLife.61312
Liu, Z. et al. Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization. Cell Host Microbe 29, 477–488 (2021).
doi: 10.1016/j.chom.2021.01.014
Andreano, E. et al. SARS-CoV-2 escape in vitro from a highly neutralizing Covid-19 convalescent plasma. Preprint at https://doi.org/10.1101/2020.12.28.424451 (2020).
Greaney, A. J. et al. Comprehensive mapping of mutations in the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human plasma antibodies. Cell Host Microbe 29, 463–476 (2021).
doi: 10.1016/j.chom.2021.02.003
Xie, X. et al. Neutralization of SARSCoV-2 spike 69/70 deletion, E484K and N501Y variants by BNT162b2 vaccine-elicited sera. Nat. Med. https://doi.org/10.1038/s41591-021-01270-4 (2021).
Wang, Z. et al. mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants. Nature https://doi.org/10.1038/s41586-021-03324-6 (2021).
Wu, K. et al. Serum neutralizing activity elicited by mRNA-1273 vaccine. N. Engl. J. Med. https://doi.org/10.1056/NEJMc2102179 (2021).
Liu, Y. et al. Neutralizing activity of BNT162b2-elicited serum. N. Engl. J. Med. https://doi.org/10.1056/NEJMc2102017 (2021).
Garcia-Beltran, W. F. et al. Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity. Cell https://doi.org/10.1016/j.cell.2021.03.013 (2021).
Wibmer, C. K. et al. SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma. Nat. Med. https://doi.org/10.1038/s41591-021-01285-x (2021).
Hoffmann, M. et al. SARS-CoV-2 variants B.1.351 and B.1.1.248: escape from therapeutic antibodies and antibodies induced by infection and vaccination. Preprint at https://doi.org/10.1101/2021.02.11.430787 (2021).
Planas, D. et al. Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies. Nat. Med. https://doi.org/10.1038/s41591-021-01318-5 (2021).
Skelly, D. T. et al. Vaccine-induced immunity provides more robust heterotypic immunity than natural infection to emerging SARS-CoV-2 variants of concern. Preprint at https://doi.org/10.21203/rs.3.rs-226857/v1 (2021).
Wang, P. et al. Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7. Nature https://doi.org/10.1038/s41586-021-03398-2 (2021).
Karim, F. et al. HIV infection alters SARSCoV-2 responsive immune parameters but not clinical outcomes in COVID-19 disease. Preprint at https://doi.org/10.1101/2020.11.23.20236828 (2020).
Gaebler, C. et al. Evolution of antibody immunity to SARS-CoV-2. Nature 591, 639–644 (2021).
doi: 10.1038/s41586-021-03207-w
Case, J. B., Bailey, A L., Kim, A. S., Chen, R. E. & Diamond, M. S. Growth, detection, quantification, and inactivation of SARS-CoV-2. Virology 548, 39–48 (2020).
doi: 10.1016/j.virol.2020.05.015
Sigal, A. et al. Cell-to-cell spread of HIV permits ongoing replication despite antiretroviral therapy. Nature 477, 95–98 (2011).
doi: 10.1038/nature10347
Shen, L. et al. Dose-response curve slope sets class-specific limits on inhibitory potential of anti-HIV drugs. Nat. Med. 14, 762–766 (2008).
doi: 10.1038/nm1777
Tarke, A. et al. Comprehensive analysis of T cell immunodominance and immunoprevalence of SARS-CoV-2 epitopes in COVID-19 cases. Cell. Rep. Med. 2, 100204 (2021).
doi: 10.1016/j.xcrm.2021.100204