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Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms
Journal article   Open access   Peer reviewed

Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms

Jessica M Weidner, Dong Jiang, Xiao-Ben Pan, Jinhong Chang, Timothy M Block and Ju-Tao Guo
Journal of virology, v 84(24), pp 12646-12657
Dec 2010
DOI: https://doi.org/10.1128/JVI.01328-10
PMID: 20943977
Featured in Collection :   UN Sustainable Development Goals @ Drexel
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https://doi.org/10.1128/jvi.01328-10View
Published, Version of Record (VoR)Open Access (License Unspecified),  Open

Abstract

Antigens, CD - genetics Antigens, CD - metabolism Blotting, Northern Blotting, Western Cells, Cultured Endocytosis Genome, Viral GPI-Linked Proteins - genetics GPI-Linked Proteins - metabolism Humans Membrane Proteins - genetics Membrane Proteins - metabolism Mutation - genetics Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - genetics RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Transcription, Genetic Vesicular Stomatitis - genetics Vesicular Stomatitis - prevention & control Vesicular Stomatitis - virology Vesicular stomatitis Indiana virus - pathogenicity Virion - physiology Virus Internalization Virus Replication - physiology
Tetherin and IFITM3 are recently identified interferon-induced cellular proteins that restrict infections by retroviruses and filoviruses and of influenza virus and flaviviruses, respectively. In our efforts to further explore their antiviral activities against other viruses and determine their antiviral mechanisms, we found that the two antiviral proteins potently inhibit the infection of vesicular stomatitis virus (VSV), a prototype member of the Rhabdoviridae family. Taking advantage of this well-studied virus infection system, we show that although both tetherin and IFITM3 are plasma membrane proteins, tetherin inhibits virion particle release from infected cells, while IFITM3 disrupts an early event after endocytosis of virion particles but before primary transcription of incoming viral genomes. Furthermore, we demonstrate that both the N-terminal 21 amino acid residues and C-terminal transmembrane region of IFITM3 are required for its antiviral activity. Collectively, our work sheds light on the mechanisms by which tetherin and IFITM3 restrict infection with rhabdoviruses and possibly other pathogenic viruses.

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