Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies

Research output: Contribution to journalArticlepeer-review

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Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies. / The CITIID-NIHR BioResource COVID-19 Collaboration; The COVID-19 Genomics UK (COG-UK) Consortium.

In: Nature, Vol. 593, No. 7857, 06.05.2021, p. 136–141.

Research output: Contribution to journalArticlepeer-review

Harvard

The CITIID-NIHR BioResource COVID-19 Collaboration & The COVID-19 Genomics UK (COG-UK) Consortium 2021, 'Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies', Nature, vol. 593, no. 7857, pp. 136–141. https://doi.org/10.1038/s41586-021-03412-7

APA

The CITIID-NIHR BioResource COVID-19 Collaboration, & The COVID-19 Genomics UK (COG-UK) Consortium (2021). Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies. Nature, 593(7857), 136–141. https://doi.org/10.1038/s41586-021-03412-7

Vancouver

The CITIID-NIHR BioResource COVID-19 Collaboration, The COVID-19 Genomics UK (COG-UK) Consortium. Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies. Nature. 2021 May 6;593(7857):136–141. https://doi.org/10.1038/s41586-021-03412-7

Author

The CITIID-NIHR BioResource COVID-19 Collaboration ; The COVID-19 Genomics UK (COG-UK) Consortium. / Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies. In: Nature. 2021 ; Vol. 593, No. 7857. pp. 136–141.

Bibtex

@article{5236bb273d0f402d905261ae3d66ca20,
title = "Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies",
abstract = "Transmission of SARS-CoV-2 is uncontrolled in many parts of the world; control is compounded in some areas by the higher transmission potential of the B.1.1.7 variant1, which has now been reported in 94 countries. It is unclear whether the response of the virus to vaccines against SARS-CoV-2 on the basis of the prototypic strain will be affected by the mutations found in B.1.1.7. Here we assess the immune responses of individuals after vaccination with the mRNA-based vaccine BNT162b22. We measured neutralizing antibody responses after the first and second immunizations using pseudoviruses that expressed the wild-type spike protein or a mutated spike protein that contained the eight amino acid changes found in the B.1.1.7 variant. The sera from individuals who received the vaccine exhibited a broad range of neutralizing titres against the wild-type pseudoviruses that were modestly reduced against the B.1.1.7 variant. This reduction was also evident in sera from some patients who had recovered from COVID-19. Decreased neutralization of the B.1.1.7 variant was also observed for monoclonal antibodies that target the N-terminal domain (9 out of 10) and the receptor-binding motif (5 out of 31), but not for monoclonal antibodies that recognize the receptor-binding domain that bind outside the receptor-binding motif. Introduction of the mutation that encodes the E484K substitution in the B.1.1.7 background to reflect a newly emerged variant of concern (VOC 202102/02) led to a more-substantial loss of neutralizing activity by vaccine-elicited antibodies and monoclonal antibodies (19 out of 31) compared with the loss of neutralizing activity conferred by the mutations in B.1.1.7 alone. The emergence of the E484K substitution in a B.1.1.7 background represents a threat to the efficacy of the BNT162b2 vaccine.",
author = "{The CITIID-NIHR BioResource COVID-19 Collaboration} and {The COVID-19 Genomics UK (COG-UK) Consortium} and Collier, {Dami A.} and {De Marco}, Anna and Ferreira, {Isabella A. T. M.} and Bo Meng and Datir, {Rawlings P.} and Walls, {Alexandra C.} and Kemp, {Steven A.} and Jessica Bassi and Dora Pinto and Chiara Silacci-fregni and Siro Bianchi and Tortorici, {M. Alejandra} and John Bowen and Katja Culap and Stefano Jaconi and Elisabetta Cameroni and Gyorgy Snell and Pizzuto, {Matteo S.} and Pellanda, {Alessandra Franzetti} and Christian Garzoni and Agostino Riva and Anne Elmer and Nathalie Kingston and Barbara Graves and Mccoy, {Laura E.} and Smith, {Kenneth G. C.} and Bradley, {John R.} and Nigel Temperton and Lourdes Ceron-gutierrez and Gabriela Barcenas-morales and William Harvey and Virgin, {Herbert W.} and Antonio Lanzavecchia and Luca Piccoli and Rainer Doffinger and Mark Wills and David Veesler and Davide Corti and Gupta, {Ravindra K.} and Andrew Beggs",
note = "Funding Information: Acknowledgements We thank the Cambridge University Hospitals NHS Trust Occupational Health Department; the NIHR Cambridge Clinical Research Facility and staff at CUH; E. Lim and G. Okecha; J. Voss for the gift of HeLa cells that stably express ACE2. R.K.G. is supported by a Wellcome Trust Senior Fellowship in Clinical Science (WT108082AIA). L.E.M. is supported by a Medical Research Council Career Development Award (MR/R008698/1). S.A.K. is supported by the Bill and Melinda Gates Foundation via PANGEA grant OPP1175094. D.A.C. is supported by a Wellcome Trust Clinical PhD Research Fellowship. K.G.C.S. is the recipient of a Wellcome Investigator Award (200871/Z/16/Z). This research was supported by the National Institute for Health Research (NIHR) Cambridge Biomedical Research Centre, the Cambridge Clinical Trials Unit (CCTU) and the NIHR BioResource. This study was supported by the National Institute of General Medical Sciences (R01GM120553 to D.V.), the National Institute of Allergy and Infectious Diseases (DP1AI158186 and HHSN272201700059C to D.V.), a Pew Biomedical Scholars Award (D.V.), an Investigators in the Pathogenesis of Infectious Disease Awards from the Burroughs Wellcome Fund (D.V.) and Fast Grants (D.V.). The views expressed are those of the authors and not necessarily those of the NIHR or the Department of Health and Social Care. I.A.T.M.F. is funded by a SANTHE award (DEL-15-006).",
year = "2021",
month = may,
day = "6",
doi = "10.1038/s41586-021-03412-7",
language = "English",
volume = "593",
pages = "136–141",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "7857",

}

RIS

TY - JOUR

T1 - Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies

AU - The CITIID-NIHR BioResource COVID-19 Collaboration

AU - The COVID-19 Genomics UK (COG-UK) Consortium

AU - Collier, Dami A.

AU - De Marco, Anna

AU - Ferreira, Isabella A. T. M.

AU - Meng, Bo

AU - Datir, Rawlings P.

AU - Walls, Alexandra C.

AU - Kemp, Steven A.

AU - Bassi, Jessica

AU - Pinto, Dora

AU - Silacci-fregni, Chiara

AU - Bianchi, Siro

AU - Tortorici, M. Alejandra

AU - Bowen, John

AU - Culap, Katja

AU - Jaconi, Stefano

AU - Cameroni, Elisabetta

AU - Snell, Gyorgy

AU - Pizzuto, Matteo S.

AU - Pellanda, Alessandra Franzetti

AU - Garzoni, Christian

AU - Riva, Agostino

AU - Elmer, Anne

AU - Kingston, Nathalie

AU - Graves, Barbara

AU - Mccoy, Laura E.

AU - Smith, Kenneth G. C.

AU - Bradley, John R.

AU - Temperton, Nigel

AU - Ceron-gutierrez, Lourdes

AU - Barcenas-morales, Gabriela

AU - Harvey, William

AU - Virgin, Herbert W.

AU - Lanzavecchia, Antonio

AU - Piccoli, Luca

AU - Doffinger, Rainer

AU - Wills, Mark

AU - Veesler, David

AU - Corti, Davide

AU - Gupta, Ravindra K.

AU - Beggs, Andrew

N1 - Funding Information: Acknowledgements We thank the Cambridge University Hospitals NHS Trust Occupational Health Department; the NIHR Cambridge Clinical Research Facility and staff at CUH; E. Lim and G. Okecha; J. Voss for the gift of HeLa cells that stably express ACE2. R.K.G. is supported by a Wellcome Trust Senior Fellowship in Clinical Science (WT108082AIA). L.E.M. is supported by a Medical Research Council Career Development Award (MR/R008698/1). S.A.K. is supported by the Bill and Melinda Gates Foundation via PANGEA grant OPP1175094. D.A.C. is supported by a Wellcome Trust Clinical PhD Research Fellowship. K.G.C.S. is the recipient of a Wellcome Investigator Award (200871/Z/16/Z). This research was supported by the National Institute for Health Research (NIHR) Cambridge Biomedical Research Centre, the Cambridge Clinical Trials Unit (CCTU) and the NIHR BioResource. This study was supported by the National Institute of General Medical Sciences (R01GM120553 to D.V.), the National Institute of Allergy and Infectious Diseases (DP1AI158186 and HHSN272201700059C to D.V.), a Pew Biomedical Scholars Award (D.V.), an Investigators in the Pathogenesis of Infectious Disease Awards from the Burroughs Wellcome Fund (D.V.) and Fast Grants (D.V.). The views expressed are those of the authors and not necessarily those of the NIHR or the Department of Health and Social Care. I.A.T.M.F. is funded by a SANTHE award (DEL-15-006).

PY - 2021/5/6

Y1 - 2021/5/6

N2 - Transmission of SARS-CoV-2 is uncontrolled in many parts of the world; control is compounded in some areas by the higher transmission potential of the B.1.1.7 variant1, which has now been reported in 94 countries. It is unclear whether the response of the virus to vaccines against SARS-CoV-2 on the basis of the prototypic strain will be affected by the mutations found in B.1.1.7. Here we assess the immune responses of individuals after vaccination with the mRNA-based vaccine BNT162b22. We measured neutralizing antibody responses after the first and second immunizations using pseudoviruses that expressed the wild-type spike protein or a mutated spike protein that contained the eight amino acid changes found in the B.1.1.7 variant. The sera from individuals who received the vaccine exhibited a broad range of neutralizing titres against the wild-type pseudoviruses that were modestly reduced against the B.1.1.7 variant. This reduction was also evident in sera from some patients who had recovered from COVID-19. Decreased neutralization of the B.1.1.7 variant was also observed for monoclonal antibodies that target the N-terminal domain (9 out of 10) and the receptor-binding motif (5 out of 31), but not for monoclonal antibodies that recognize the receptor-binding domain that bind outside the receptor-binding motif. Introduction of the mutation that encodes the E484K substitution in the B.1.1.7 background to reflect a newly emerged variant of concern (VOC 202102/02) led to a more-substantial loss of neutralizing activity by vaccine-elicited antibodies and monoclonal antibodies (19 out of 31) compared with the loss of neutralizing activity conferred by the mutations in B.1.1.7 alone. The emergence of the E484K substitution in a B.1.1.7 background represents a threat to the efficacy of the BNT162b2 vaccine.

AB - Transmission of SARS-CoV-2 is uncontrolled in many parts of the world; control is compounded in some areas by the higher transmission potential of the B.1.1.7 variant1, which has now been reported in 94 countries. It is unclear whether the response of the virus to vaccines against SARS-CoV-2 on the basis of the prototypic strain will be affected by the mutations found in B.1.1.7. Here we assess the immune responses of individuals after vaccination with the mRNA-based vaccine BNT162b22. We measured neutralizing antibody responses after the first and second immunizations using pseudoviruses that expressed the wild-type spike protein or a mutated spike protein that contained the eight amino acid changes found in the B.1.1.7 variant. The sera from individuals who received the vaccine exhibited a broad range of neutralizing titres against the wild-type pseudoviruses that were modestly reduced against the B.1.1.7 variant. This reduction was also evident in sera from some patients who had recovered from COVID-19. Decreased neutralization of the B.1.1.7 variant was also observed for monoclonal antibodies that target the N-terminal domain (9 out of 10) and the receptor-binding motif (5 out of 31), but not for monoclonal antibodies that recognize the receptor-binding domain that bind outside the receptor-binding motif. Introduction of the mutation that encodes the E484K substitution in the B.1.1.7 background to reflect a newly emerged variant of concern (VOC 202102/02) led to a more-substantial loss of neutralizing activity by vaccine-elicited antibodies and monoclonal antibodies (19 out of 31) compared with the loss of neutralizing activity conferred by the mutations in B.1.1.7 alone. The emergence of the E484K substitution in a B.1.1.7 background represents a threat to the efficacy of the BNT162b2 vaccine.

UR - http://www.scopus.com/inward/record.url?scp=85102509491&partnerID=8YFLogxK

U2 - 10.1038/s41586-021-03412-7

DO - 10.1038/s41586-021-03412-7

M3 - Article

VL - 593

SP - 136

EP - 141

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7857

ER -