Arbidol inhibits viral entry by interfering with clathrin-dependent trafficking

被引：77

作者：

Blaising, Julie ^{[1
]}

Levy, Pierre L. ^{[2
]}

Polyak, Stephen J. ^{[3
]}

Stanifer, Megan ^{[4
,5
]}

Boulant, Steeve ^{[4
,5
]}

Pecheur, Eve-Isabelle ^{[1
]}

机构：

[1] Univ Lyon, CNRS, IBCP, UMR 5086, F-69424 Lyon 03, France

[2] Univ Lyon, INSERM, CRCL, CNRS 5286,U1052, F-69424 Lyon 03, France

[3] Univ Washington, Dept Lab Med & Global Hlth, Seattle, WA 98195 USA

[4] Heidelberg Univ, CHS Nachwuchsgrp CellNetworks Cluster, Dept Infect Dis, Heidelberg, Germany

[5] Heidelberg Univ, DKFZ, Heidelberg, Germany

来源：

ANTIVIRAL RESEARCH | 2013年 / 100卷 / 01期

关键词：

Hepatitis C virus; Vesicular stomatitis virus; Reovirus; Arbidol; Broad spectrum antiviral; Entry; HEPATITIS-C-VIRUS; RESPIRATORY VIRUSES; ANTIVIRAL ACTIVITY; REOVIRUS; ENDOCYTOSIS; MECHANISM; FUSION;

D O I：

10.1016/j.antiviral.2013.08.008

中图分类号：

R9 [药学];

学科分类号：

100702 [药剂学];

摘要：

Arbidol (ARB) is a broad-spectrum antiviral displaying activity against a number of enveloped and non-enveloped viruses. It was described as a viral entry inhibitor and shown to interact at the molecular level with lipid membranes and viral fusion glycoproteins to impede viral entry and fusion. However its mechanism of action at the cellular level remains unknown. Here, by using live-cell confocal imaging and the hepatitis C virus as a model virus, we show that ARB affects clathrin-mediated endocytosis by impeding dynamin-2-induced membrane scission. Moreover it induces the intracellular accumulation of clathrin-coated structures where viral particles are trapped. Collectively, our results shed light on the mechanistic aspects of ARB antiviral activity and suggest that ARB could prevent cell infection by viruses that enter through clathrin-mediated endocytosis. (C) 2013 Elsevier By. All rights reserved.

引用

页码：215 / 219

页数：5

共 21 条

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