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J Med Virol. The anti-HIV Drug Nelfinavir Mesylate (Viracept) is a Potent Inhibitor of Cell Fusion Caused by the SARS-CoV-2 Spike (S) Glycoprotein Wa

tetano

Editor, Senior Moderator
J Med Virol. 2020 May 6. doi: 10.1002/jmv.25985. [Epub ahead of print]
The anti-HIV Drug Nelfinavir Mesylate (Viracept) is a Potent Inhibitor of Cell Fusion Caused by the SARS-CoV-2 Spike (S) Glycoprotein Warranting further Evaluation as an Antiviral against COVID-19 infections.


Musarrat F[SUP]1,[/SUP][SUP]2[/SUP], Chouljenko V[SUP]1,[/SUP][SUP]2[/SUP], Dahal A[SUP]3[/SUP], Nabi R[SUP]1,[/SUP][SUP]2[/SUP], Chouljenko T[SUP]4[/SUP], Jois SD[SUP]3[/SUP], Kousoulas KG[SUP]1,[/SUP][SUP]2[/SUP].

Author information




Abstract

SARS coronavirus-2 (SARS CoV-2) is the causative agent of the Coronavirus Disease-2019 (COVID-19) pandemic. Coronaviruses enter cells via fusion of the viral envelope with the plasma membrane and/or via fusion of the viral envelope with endosomal membranes after virion endocytosis. The Spike (S) glycoprotein is a major determinant of virus infectivity. Herein, we show that transient expression of the SARS CoV-2 S glycoprotein in Vero cells caused extensive cell fusion (formation of syncytia) in comparison to limited cell fusion caused by the SARS CoV S glycoprotein. Both S glycoproteins were detected intracellularly and on transfected Vero cell surfaces. These results are in agreement with published pathology observations of extensive syncytial formation in lung tissues of COVID-19 patients. These results suggest that SARS CoV-2 is able to spread from cell-to-cell much more efficiently than SARS-CoV effectively avoiding extracellular neutralizing antibodies. A systematic screening of several drugs including cardiac glycosides and kinase inhibitors and inhibitors of HIV entry revealed that only the FDA approved HIV-protease inhibitor, nelfinavir mesylate (Viracept) drastically inhibited Sn and So-mediated cell fusion with complete inhibition at a 10 μM concentration. In silico docking experiments suggested the possibility that nelfinavir may bind inside the S trimer structure, proximal to the S2 amino terminus directly inhibiting Sn and So-mediated membrane fusion. Also, it is possible that nelfinavir may act to inhibit S proteolytic processing within cells. These results warrant further investigations of the potential of nelfinavir mesylate to inhibit virus spread at early times after SARS CoV-2 symptoms appear. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.



KEYWORDS:

Antiviral agents; Cell fusion; Cellular Effect; Coronavirus; Entry inhibitors; Fusion protein; Glycoproteins; Infection; SARS coronavirus; Virus classification


PMID:32374457DOI:10.1002/jmv.25985
 
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