» Articles » PMID: 32272173

Coronavirus Membrane Fusion Mechanism Offers a Potential Target for Antiviral Development

Overview
Journal Antiviral Res
Publisher Elsevier
Date 2020 Apr 10
PMID 32272173
Citations 417
Authors
Affiliations
Soon will be listed here.
Abstract

The coronavirus disease 2019 (COVID-19) pandemic has focused attention on the need to develop effective therapies against the causative agent, SARS-CoV-2, and also against other pathogenic coronaviruses (CoV) that have emerged in the past or might appear in future. Researchers are therefore focusing on steps in the CoV replication cycle that may be vulnerable to inhibition by broad-spectrum or specific antiviral agents. The conserved nature of the fusion domain and mechanism across the CoV family make it a valuable target to elucidate and develop pan-CoV therapeutics. In this article, we review the role of the CoV spike protein in mediating fusion of the viral and host cell membranes, summarizing the results of research on SARS-CoV, MERS-CoV, and recent peer-reviewed studies of SARS-CoV-2, and suggest that the fusion mechanism be investigated as a potential antiviral target. We also provide a supplemental file containing background information on the biology, epidemiology, and clinical features of all human-infecting coronaviruses, along with a phylogenetic tree of these coronaviruses.

Citing Articles

Molecular imaging of viral pathogenesis and opportunities for the future.

Kelly B, Boudreau J, Beyea S, Brewer K Npj Imaging. 2025; 3(1):3.

PMID: 39872292 PMC: 11761071. DOI: 10.1038/s44303-024-00056-w.


SARS-CoV-2 FP1 Destabilizes Lipid Membranes and Facilitates Pore Formation.

Sumarokova M, Pavlov R, Lavushchenko T, Vasilenko E, Kozhemyakin G, Fedorov O Int J Mol Sci. 2025; 26(2).

PMID: 39859399 PMC: 11765642. DOI: 10.3390/ijms26020686.


Probing SARS-CoV-2 membrane binding peptide via single-molecule AFM-based force spectroscopy.

Zhang Q, Rosa R, Ray A, Durlet K, Dorrazehi G, Bernardi R Nat Commun. 2025; 16(1):6.

PMID: 39747000 PMC: 11696146. DOI: 10.1038/s41467-024-55358-9.


Dimethoxycurcumin Acidifies Endolysosomes and Inhibits SARS-CoV-2 Entry.

Khan N, Afghah Z, Baral A, Geiger J, Chen X Front Virol. 2024; 2.

PMID: 39677976 PMC: 11638979. DOI: 10.3389/fviro.2022.923018.


Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infection.

Zhang Y, Schmick S, Xie L, Ghosh U, Weliky D Proc Natl Acad Sci U S A. 2024; 121(50):e2402953121.

PMID: 39621921 PMC: 11648660. DOI: 10.1073/pnas.2402953121.


References
1.
Yuan K, Yi L, Chen J, Qu X, Qing T, Rao X . Suppression of SARS-CoV entry by peptides corresponding to heptad regions on spike glycoprotein. Biochem Biophys Res Commun. 2004; 319(3):746-52. PMC: 7111000. DOI: 10.1016/j.bbrc.2004.05.046. View

2.
Madu I, Belouzard S, Whittaker G . SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion. Virology. 2009; 393(2):265-71. PMC: 3594805. DOI: 10.1016/j.virol.2009.07.038. View

3.
Jaimes J, Millet J, Stout A, Andre N, Whittaker G . A Tale of Two Viruses: The Distinct Spike Glycoproteins of Feline Coronaviruses. Viruses. 2020; 12(1). PMC: 7019228. DOI: 10.3390/v12010083. View

4.
Dyall J, Coleman C, Hart B, Venkataraman T, Holbrook M, Kindrachuk J . Repurposing of clinically developed drugs for treatment of Middle East respiratory syndrome coronavirus infection. Antimicrob Agents Chemother. 2014; 58(8):4885-93. PMC: 4136000. DOI: 10.1128/AAC.03036-14. View

5.
Zhou P, Yang X, Wang X, Hu B, Zhang L, Zhang W . A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020; 579(7798):270-273. PMC: 7095418. DOI: 10.1038/s41586-020-2012-7. View