Reduced sensitivity of SARS-CoV-2 variant Delta to antibody neutralization

Nature - Tập 596 Số 7871 - Trang 276-280 - 2021
Delphine Planas1, David Veyer2, Artem Baidaliuk3, Isabelle Staropoli1, Florence Guivel‐Benhassine1, Maaran Michael Rajah1, Cyril Planchais4, Françoise Porrot1, Nicolas Robillard5, Julien Puech5, Matthieu Prot3, Floriane Gallais6, Pierre Gantner6, Aurélie Velay6, J. Le Guen7, Najiby Kassis‐Chikhani8, Dhiaeddine Edriss5, Laurent Bélec5, Aymeric Sève9, Laura Courtellemont9, Hélène Péré2, Laurent Hocqueloux9, Samira Fafi‐Kremer6, Thiérry Prazuck9, Hugo Mouquet4, Timothée Bruel10, Etienne Simon‐Lorière3, F.A. Rey11, Olivier Schwartz10
1Virus and Immunity Unit, Department of Virology, Institut Pasteur, CNRS UMR 3569, Paris, France
2INSERM, Functional Genomics of Solid Tumors (FunGeST), Centre de Recherche des Cordeliers, Université de Paris and Sorbonne Université, Paris, France
3G5 Evolutionary genomics of RNA viruses, Department of Virology, Institut Pasteur, Paris, France
4Laboratory of Humoral Immunology, Department of Immunology, Institut Pasteur, INSERM U1222, Paris, France
5Laboratoire de Virologie, Service de Microbiologie, Hôpital Européen Georges Pompidou, Assistance Publique des Hôpitaux de Paris, Paris, France
6CHU de Strasbourg, Laboratoire de Virologie, Strasbourg, France
7Service de Gériatrie, Hôpital Européen Georges Pompidou, Assistance Publique des Hôpitaux de Paris, Paris, France
8Unité d'Hygiène Hospitalière, Service de Microbiologie, Hôpital Européen Georges Pompidou, Assistance Publique des Hôpitaux de Paris, Paris, France
9CHR d'Orléans, service de maladies infectieuses, Orléans, France
10Vaccine Research Institute, Creteil, France
11Structural Virology Unit, Department of Virology, Institut Pasteur, CNRS UMR 3569, Paris, France

Tóm tắt

Từ khóa


Tài liệu tham khảo

Yadav, P. D. et al. Neutralization of variant under investigation B.1.617 with sera of BBV152 vaccinees. Clin. Infect. Dis. https://doi.org/10.1093/cid/ciab411 (2021).

Ferreira, I. et al. SARS-CoV-2 B.1.617 emergence and sensitivity to vaccine-elicited antibodies. Preprint at https://doi.org/10.1101/2021.05.08.443253 (2021).

Hoffmann, M. et al. SARS-CoV-2 variant B.1.617 is resistant to Bamlanivimab and evades antibodies induced by infection and vaccination. Cell Rep. https://doi.org/10.1016/j.celrep.2021.109415 (2021).

Cherian, S. et al. Convergent evolution of SARS-CoV-2 spike mutations, L452R, E484Q and P681R, in the second wave of COVID-19 in Maharashtra, India. Preprint at https://doi.org/10.1101/2021.04.22.440932 (2021).

Edara, V.-V. et al. Infection and vaccine-induced neutralizing-antibody responses to the SARS-CoV-2 B.1.617 variants. New Eng. J. Med. https://doi.org/10.1056/NEJMc2107799 (2021).

Public Health England. Variants: distribution of case data, 11 June 2021. https://www.gov.uk/government/publications/covid-19-variants-genomically-confirmed-case-numbers/variants-distribution-of-case-data-11-june-2021 (2021).

Tada, T. et al. The spike proteins of SARS-CoV-2 B.1.617 and B.1.618 variants identified in India provide partial resistance to vaccine-elicited and therapeutic monoclonal antibodies. Preprint at https://doi.org/10.1101/2021.05.14.444076 (2021).

Liu, J. et al. BNT162b2-elicited neutralization of B.1.617 and other SARS-CoV-2 variants. Nature https://doi.org/10.1038/s41586-021-03693-y (2021).

Wall, E. C. et al. Neutralising antibody activity against SARS-CoV-2 VOCs B.1.617.2 and B.1.351 by BNT162b2 vaccination. Lancet 397, 2331–2333 (2021).

Buchrieser, J. et al. Syncytia formation by SARS-CoV-2-infected cells. EMBO J. 39, e106267 (2020).

Planas, D. et al. Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies. Nat. Med. 27, 917–924 (2021).

Rambaut, A. et al. A dynamic nomenclature proposal for SARS-CoV-2 lineages to assist genomic epidemiology. Nat. Microbiol. 5, 1403–1407 (2020).

Plante, J. A. et al. The variant gambit: COVID-19’s next move. Cell Host Microbe 29, 508–515 (2021).

Centers for Disease Control and Prevention. SARS-CoV-2 variant classifications and definitions. https://www.cdc.gov/coronavirus/2019-ncov/cases-updates/variant-surveillance/variant-info.html (2021).

McCallum, M. et al. N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2. Cell 184, 2332–2347 (2021).

Starr, T. N., Greaney, A. J., Dingens, A. S. & Bloom, J. D. Complete map of SARS-CoV-2 RBD mutations that escape the monoclonal antibody LY-CoV555 and its cocktail with LY-CoV016. Cell Rep. Med. 2, 100255 (2021).

Barnes, C. O. et al. SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies. Nature 588, 682–687 (2020).

Taylor, P. C. et al. Neutralizing monoclonal antibodies for treatment of COVID-19. Nat. Rev. Immunol. 21, 382–393 (2021).

Starr, T. N. et al. Prospective mapping of viral mutations that escape antibodies used to treat COVID-19. Science 371, 850–854 (2021).

Liu, L. et al. Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike. Nature 584, 450–456 (2020).

Wang, P. et al. Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7. Nature 593, 130–135 (2021).

Fafi-Kremer, S. et al. Serologic responses to SARS-CoV-2 infection among hospital staff with mild disease in eastern France. EBioMedicine 59, 102915 (2020).

Gallais, F. et al. Anti-SARS-CoV-2 antibodies persist for up to 13 months and reduce risk of reinfection. Preprint at https://doi.org/10.1101/2021.05.07.21256823 (2021).

Krammer, F. et al. Antibody responses in seropositive persons after a single dose of SARS-CoV-2 mRNA vaccine. N. Engl. J. Med. 384, 1372–1374 (2021).

Khoury, D. S. et al. Neutralizing antibody levels are highly predictive of immune protection from symptomatic SARS-CoV-2 infection. Nat. Med. (2021).

Bernal, J. L. et al. Effectiveness of COVID-19 vaccines against the B.1.617.2 variant. Preprint at https://doi.org/10.1101/2021.05.22.21257658 (2021).

Hadfield, J. et al. Nextstrain: real-time tracking of pathogen evolution. Bioinformatics 34, 4121–4123 (2018).

Cai, Y. et al. Distinct conformational states of SARS-CoV-2 spike protein. Science 369, 1586–1592 (2020).

Lorin, V. & Mouquet, H. Efficient generation of human IgA monoclonal antibodies. J. Immunol. Methods 422, 102–110 (2015).

Tzou, P. L. et al. Coronavirus antiviral research database (CoV-RDB): an online database designed to facilitate comparisons between candidate anti-coronavirus compounds. Viruses 12, 1006 (2020).