SARS-CoV-2 variant B.1.1.7 is susceptible to neutralizing antibodies elicited by ancestral Spike vaccines.


Journal

bioRxiv : the preprint server for biology
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187

Informations de publication

Date de publication:
29 Jan 2021
Historique:
entrez: 3 2 2021
pubmed: 4 2 2021
medline: 4 2 2021
Statut: epublish

Résumé

The SARS-CoV-2 Spike glycoprotein mediates virus entry and is a major target for neutralizing antibodies. All current vaccines are based on the ancestral Spike with the goal of generating a protective neutralizing antibody response. Several novel SARS-CoV-2 variants with multiple Spike mutations have emerged, and their rapid spread and potential for immune escape have raised concerns. One of these variants, first identified in the United Kingdom, B.1.1.7 (also called VUI202012/01), contains eight Spike mutations with potential to impact antibody therapy, vaccine efficacy and risk of reinfection. Here we employed a lentivirus-based pseudovirus assay to show that variant B.1.1.7 remains sensitive to neutralization, albeit at moderately reduced levels (~2-fold), by serum samples from convalescent individuals and recipients of two different vaccines based on ancestral Spike: mRNA-1273 (Moderna), and protein nanoparticle NVX-CoV2373 (Novavax). Some monoclonal antibodies to the receptor binding domain (RBD) of Spike were less effective against the variant while others were largely unaffected. These findings indicate that B.1.1.7 is not a neutralization escape variant that would be a major concern for current vaccines, or for an increased risk of reinfection.

Identifiants

pubmed: 33532764
doi: 10.1101/2021.01.27.428516
pmc: PMC7852228
pii:
doi:

Types de publication

Preprint

Langues

eng

Commentaires et corrections

Type : UpdateIn

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Auteurs

Xiaoying Shen (X)

Department of Surgery, Duke University School of Medicine, Durham, NC, USA.
Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC, USA.

Haili Tang (H)

Department of Surgery, Duke University School of Medicine, Durham, NC, USA.

Charlene McDanal (C)

Department of Surgery, Duke University School of Medicine, Durham, NC, USA.

Kshitij Wagh (K)

Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM USA.

Will Fischer (W)

Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM USA.

James Theiler (J)

Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM USA.

Hyejin Yoon (H)

Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM USA.

Dapeng Li (D)

Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC, USA.

Barton F Haynes (BF)

Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC, USA.
Department of Medicine, Duke University Medical Center, Durham, NC, USA.

Kevin O Sanders (KO)

Department of Surgery, Duke University School of Medicine, Durham, NC, USA.
Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC, USA.
Department of Medicine, Duke University Medical Center, Durham, NC, USA.

Sandrasegaram Gnanakaran (S)

Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM USA.

Nick Hengartner (N)

Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM USA.

Rolando Pajon (R)

Moderna Inc., Cambridge, MA, USA.

Gale Smith (G)

Novavax, Inc., Gaithersburg, MD, USA.

Filip Dubovsky (F)

Novavax, Inc., Gaithersburg, MD, USA.

Gregory M Glenn (GM)

Novavax, Inc., Gaithersburg, MD, USA.

Bette Korber (B)

Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM USA.

David C Montefiori (DC)

Department of Surgery, Duke University School of Medicine, Durham, NC, USA.
Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC, USA.

Classifications MeSH