Cited by 2,740SARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections StudiesVirology and Viral Diseases

Structure, Function, and Evolution of Coronavirus Spike Proteins

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Li, Fang·2016·Annual Review of Virology

Abstract

The coronavirus spike protein is a multifunctional molecular machine that mediates coronavirus entry into host cells. It first binds to a receptor on the host cell surface through its S1 subunit and then fuses viral and host membranes through its S2 subunit. Two domains in S1 from different coronaviruses recognize a variety of host receptors, leading to viral attachment. The spike protein exists in two structurally distinct conformations, prefusion and postfusion. The transition from prefusion to postfusion conformation of the spike protein must be triggered, leading to membrane fusion. This article reviews current knowledge about the structures and functions of coronavirus spike proteins, illustrating how the two S1 domains recognize different receptors and how the spike proteins are regulated to undergo conformational transitions. I further discuss the evolution of these two critical functions of coronavirus spike proteins, receptor recognition and membrane fusion, in the context of the corresponding functions from other viruses and host cells.

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  • Before host cell contact, spike is in a metastable pre-fusion trimer that rearranges substantially during virus-cell fusion.

    “Prior to contact with the host cell, the S protein is in a metastable pre-fusion conformation and the trimer undergoes substantial rearrangement at the time of virus–cell fusion150,151.”

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  1. [116]Xu Y Liu Y Lou Z Qin L Li X 2004 Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core J Biol Chem 279 30514 22 15123674 PMC7982547

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Authors
Li, F.
Affiliations
University of Minnesota (US)
Corresponding author
Li, Fang
Venue
Annual Review of Virology
Published
2016-09-29
Volume
3
Issue
1
Pages
237-261
ISSN
  • 2327-056X (ISSN-L)
  • 2327-0578
OpenAlex
W2513547424
Cited by
2,740
References
151
Citations by year
2026: 76 · 2025: 137 · 2024: 183 · 2023: 251 · 2022: 441 · 2021: 733 · 2020: 860 · 2019: 26 · 2018: 19 · 2017: 8 · 2016: 3 · 2012: 1
FWCI
2.88
Type
journal article
Language
en
Open access
Locations
  • Annual Review of Virology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute of Allergy and Infectious Diseases (R01AI110700, R01AI089728)
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, receptor recognition, host cell receptors, viral evolution, spike protein structure, membrane fusion
MeSH terms
Humans, Membrane Fusion, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins, Coronavirus, Coronavirus Infections, Virus Attachment, Virus Internalization, Spike Glycoprotein, Coronavirus

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