An Engineered Receptor-Binding Domain Improves the Immunogenicity of Multivalent SARS-CoV-2 Vaccines.


Journal

mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231

Informations de publication

Date de publication:
11 05 2021
Historique:
entrez: 12 5 2021
pubmed: 13 5 2021
medline: 25 5 2021
Statut: epublish

Résumé

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S) protein mediates viral entry into cells expressing angiotensin-converting enzyme 2 (ACE2). The S protein engages ACE2 through its receptor-binding domain (RBD), an independently folded 197-amino-acid fragment of the 1,273-amino-acid S-protein protomer. The RBD is the primary SARS-CoV-2 neutralizing epitope and a critical target of any SARS-CoV-2 vaccine. Here, we show that this RBD conjugated to each of two carrier proteins elicited more potent neutralizing responses in immunized rodents than did a similarly conjugated proline-stabilized S-protein ectodomain. Nonetheless, the native RBD is expressed inefficiently, limiting its usefulness as a vaccine antigen. However, we show that an RBD engineered with four novel glycosylation sites (gRBD) is expressed markedly more efficiently and generates a more potent neutralizing responses as a DNA vaccine antigen than the wild-type RBD or the full-length S protein, especially when fused to multivalent carriers, such as a

Identifiants

pubmed: 33975938
pii: mBio.00930-21
doi: 10.1128/mBio.00930-21
pmc: PMC8262850
pii:
doi:

Substances chimiques

COVID-19 Vaccines 0
Receptors, Coronavirus 0
Spike Glycoprotein, Coronavirus 0
Vaccines, Conjugate 0
Vaccines, Synthetic 0
spike protein, SARS-CoV-2 0
Angiotensin-Converting Enzyme 2 EC 3.4.17.23

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIAID NIH HHS
ID : R01 AI129868
Pays : United States

Commentaires et corrections

Type : UpdateOf

Informations de copyright

Copyright © 2021 Guo et al.

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Auteurs

Yan Guo (Y)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Wenhui He (W)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Huihui Mou (H)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Lizhou Zhang (L)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Jing Chang (J)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Shoujiao Peng (S)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Amrita Ojha (A)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Rubens Tavora (R)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Mark S Parcells (MS)

Department of Animal and Food Sciences, University of Delaware, Newark, Delaware, USA.

Guangxiang Luo (G)

Department of Microbiology, University of Alabama at Birmingham School of Medicine, Birmingham, Alabama, USA.

Wenhui Li (W)

National Institute of Biological Sciences, Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing, China.

Guocai Zhong (G)

Scripps Research SZBL Chemical Biology Institute, Shenzhen Bay Laboratory, Shenzhen, China.
School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.

Hyeryun Choe (H)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA.

Michael Farzan (M)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA mfarzan@scripps.edu bquinlan@scripps.edu.

Brian D Quinlan (BD)

Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, Florida, USA mfarzan@scripps.edu bquinlan@scripps.edu.

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Classifications MeSH