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10.1002/jmv.25985

http://scihub22266oqcxt.onion/10.1002/jmv.25985
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32374457!7267418!32374457
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suck abstract from ncbi


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pmid32374457      J+Med+Virol 2020 ; 92 (10): 2087-2095
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  • The anti-HIV drug nelfinavir mesylate (Viracept) is a potent inhibitor of cell fusion caused by the SARSCoV-2 spike (S) glycoprotein warranting further evaluation as an antiviral against COVID-19 infections #MMPMID32374457
  • Musarrat F; Chouljenko V; Dahal A; Nabi R; Chouljenko T; Jois SD; Kousoulas KG
  • J Med Virol 2020[Oct]; 92 (10): 2087-2095 PMID32374457show ga
  • Severe acute respiratory syndrome 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 the 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 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 syncytia formation in lung tissues of patients with COVID-19. These results suggest that SARS CoV-2 is able to spread from cell-to-cell much more efficiently than SARS effectively avoiding extracellular neutralizing antibodies. A systematic screening of several drugs including cardiac glycosides and kinase inhibitors and inhibitors of human immunodeficiency virus (HIV) entry revealed that only the FDA-approved HIV protease inhibitor, nelfinavir mesylate (Viracept) drastically inhibited S-n- and S-o-mediated cell fusion with complete inhibition at a 10-muM 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 S-n- and S-o-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.
  • |Animals[MESH]
  • |Anti-HIV Agents/chemistry/*pharmacology[MESH]
  • |Binding Sites[MESH]
  • |COVID-19 Drug Treatment[MESH]
  • |Cell Fusion[MESH]
  • |Chlorocebus aethiops[MESH]
  • |Giant Cells/drug effects/pathology/virology[MESH]
  • |Humans[MESH]
  • |Membrane Fusion/*drug effects[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Nelfinavir/chemistry/*pharmacology[MESH]
  • |Plasmids/chemistry/metabolism[MESH]
  • |Protein Binding[MESH]
  • |Protein Interaction Domains and Motifs[MESH]
  • |Recombinant Proteins/chemistry/genetics/metabolism[MESH]
  • |SARS-CoV-2/*drug effects/pathogenicity/physiology[MESH]
  • |Severe acute respiratory syndrome-related coronavirus/*drug effects/pathogenicity/physiology[MESH]
  • |Spike Glycoprotein, Coronavirus/*antagonists & inhibitors/chemistry/genetics/metabolism[MESH]
  • |Vero Cells[MESH]


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