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

Autor: Collier DA; Cambridge Institute of Therapeutic Immunology & Infectious Disease, Cambridge, UK.; Department of Medicine, University of Cambridge, Cambridge, UK.; Division of Infection and Immunity, University College London, London, UK., De Marco A; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Ferreira IATM; Cambridge Institute of Therapeutic Immunology & Infectious Disease, Cambridge, UK.; Department of Medicine, University of Cambridge, Cambridge, UK., Meng B; Cambridge Institute of Therapeutic Immunology & Infectious Disease, Cambridge, UK.; Department of Medicine, University of Cambridge, Cambridge, UK., Datir RP; Cambridge Institute of Therapeutic Immunology & Infectious Disease, Cambridge, UK.; Department of Medicine, University of Cambridge, Cambridge, UK.; Division of Infection and Immunity, University College London, London, UK., Walls AC; Department of Biochemistry, University of Washington, Seattle, WA, USA., Kemp SA; Cambridge Institute of Therapeutic Immunology & Infectious Disease, Cambridge, UK.; Department of Medicine, University of Cambridge, Cambridge, UK.; Division of Infection and Immunity, University College London, London, UK., Bassi J; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Pinto D; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Silacci-Fregni C; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Bianchi S; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Tortorici MA; Department of Biochemistry, University of Washington, Seattle, WA, USA., Bowen J; Department of Biochemistry, University of Washington, Seattle, WA, USA., Culap K; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Jaconi S; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Cameroni E; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Snell G; Vir Biotechnology, San Francisco, CA, USA., Pizzuto MS; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Pellanda AF; Clinic of Internal Medicine and Infectious Diseases, Clinica Luganese Moncucco, Lugano, Switzerland., Garzoni C; Clinic of Internal Medicine and Infectious Diseases, Clinica Luganese Moncucco, Lugano, Switzerland., Riva A; Division of Infectious Diseases, Luigi Sacco Hospital, University of Milan, Milan, Italy., Elmer A; NIHR Cambridge Clinical Research Facility, Cambridge, UK., Kingston N; NIHR Bioresource, Cambridge, UK., Graves B; NIHR Bioresource, Cambridge, UK., McCoy LE; Division of Infection and Immunity, University College London, London, UK., Smith KGC; Cambridge Institute of Therapeutic Immunology & Infectious Disease, Cambridge, UK.; Department of Medicine, University of Cambridge, Cambridge, UK., Bradley JR; Department of Medicine, University of Cambridge, Cambridge, UK.; NIHR Bioresource, Cambridge, UK., Temperton N; University of Kent, Canturbury, UK., Ceron-Gutierrez L; Department of Clinical Biochemistry and Immunology, Addenbrooke's Hospital, Cambridge, UK., Barcenas-Morales G; Department of Clinical Biochemistry and Immunology, Addenbrooke's Hospital, Cambridge, UK.; Laboratorio de Inmunologia, UNAM, Cuautitlán, Mexico., Harvey W; Institute of Biodiversity, University of Glasgow, Glasgow, UK., Virgin HW; Vir Biotechnology, San Francisco, CA, USA., Lanzavecchia A; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Piccoli L; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland., Doffinger R; Department of Clinical Biochemistry and Immunology, Addenbrooke's Hospital, Cambridge, UK.; Department of Haematology, University of Cambridge, Cambridge, UK., Wills M; Department of Medicine, University of Cambridge, Cambridge, UK., Veesler D; Department of Biochemistry, University of Washington, Seattle, WA, USA., Corti D; Humabs Biomed SA, a subsidiary of Vir Biotechnology, Bellinzona, Switzerland. dcorti@vir.bio., Gupta RK; Cambridge Institute of Therapeutic Immunology & Infectious Disease, Cambridge, UK. rkg20@cam.ac.uk.; Department of Medicine, University of Cambridge, Cambridge, UK. rkg20@cam.ac.uk.; Department of Haematology, University of Cambridge, Cambridge, UK. rkg20@cam.ac.uk.; University of KwaZulu Natal, Durban, South Africa. rkg20@cam.ac.uk.; Africa Health Research Institute, Durban, South Africa. rkg20@cam.ac.uk.; Department of Infectious Diseases, Cambridge University Hospitals NHS Trust, Cambridge, UK. rkg20@cam.ac.uk.
Jazyk: angličtina
Zdroj: Nature [Nature] 2021 May; Vol. 593 (7857), pp. 136-141. Date of Electronic Publication: 2021 Mar 11.
DOI: 10.1038/s41586-021-03412-7
Abstrakt: 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 variant 1 , 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 BNT162b2 2 . 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.
Databáze: MEDLINE
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