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Cited by 1,368SARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections StudiesVirology and Viral Diseases

Mechanisms of Coronavirus Cell Entry Mediated by the Viral Spike Protein

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Belouzard, Sandrine, Millet, Jean K., Licitra, Beth N., Whittaker, Gary R.·2012·Viruses
DOI 10.3390/v4061011PMC PMC3397359
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Abstract

Coronaviruses are enveloped positive-stranded RNA viruses that replicate in the cytoplasm. To deliver their nucleocapsid into the host cell, they rely on the fusion of their envelope with the host cell membrane. The spike glycoprotein (S) mediates virus entry and is a primary determinant of cell tropism and pathogenesis. It is classified as a class I fusion protein, and is responsible for binding to the receptor on the host cell as well as mediating the fusion of host and viral membranes—A process driven by major conformational changes of the S protein. This review discusses coronavirus entry mechanisms focusing on the different triggers used by coronaviruses to initiate the conformational change of the S protein: receptor binding, low pH exposure and proteolytic activation. We also highlight commonalities between coronavirus S proteins and other class I viral fusion proteins, as well as distinctive features that confer distinct tropism, pathogenicity and host interspecies transmission characteristics to coronaviruses.

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  • The SARS-CoV-2 S glycoprotein mediates host cell attachment and is required for viral entry.

    “The S glycoprotein mediates host cell attachment and is required for viral entry3; it is the primary vaccine target for many candidate SARS-CoV-2 vaccines.4-7”

    From An mRNA Vaccine against SARS-CoV-2 — Preliminary Report (2020) · cites this paper as [3]

    Section 2, “Spike Protein” (page unavailable), says coronavirus spike proteins have an S1 domain responsible for receptor binding and an S2 domain responsible for fusion, supporting the attachment-and-entry mechanism. The paper does not address SARS-CoV-2 specifically, so it does not directly establish the claim for that virus. The vaccine-target statement is attributed to other citations, not this source. (LLM, conf=0.85)

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Cited by

Sorted by citations

Authors
Belouzard, S., Millet, J. K., Licitra, B. N., & Whittaker, G. R.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • Cornell University (US)
Corresponding author
Whittaker, Gary R.
ORCID
Venue
Viruses
Publisher
MDPI AG
Published
2012-06-20
Volume
4
Issue
6
Pages
1011-1033
ISSN
1999-4915 (ISSN-L)
DOI
10.3390/v4061011
PMC
PMC3397359
OpenAlex
W2105149323
Cited by
1,368
References
2
Citations by year
2026: 38 · 2025: 45 · 2024: 78 · 2023: 144 · 2022: 183 · 2021: 345 · 2020: 356 · 2019: 33 · 2018: 25 · 2017: 32 · 2016: 29 · 2015: 16 · 2014: 26 · 2013: 17 · 2012: 1
FWCI
2.39
Type
journal article
Language
en
Open access
Licence
Locations
  • Viruses (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
  • LillOA (Université de Lille (University Of Lille)) (submittedVersion, other-oa)
Funders
  • Morris Animal Foundation
  • Winn Feline Foundation
  • National Institute of Allergy and Infectious Diseases (R21 AI1076258, R21AI107258)
Topics
  • Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
  • Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
Keywords
coronavirus, spike protein, viral entry, membrane fusion, class I fusion proteins, receptor binding, proteolytic activation, conformational change, cell tropism, host range, pathogenesis, interspecies transmission, SARS-CoV-2
MeSH terms
Animals, Humans, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins, Viral Fusion Proteins, Coronavirus, Virus Internalization, Viral Tropism, Spike Glycoprotein, Coronavirus

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