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Endoplasmic reticulum chaperone gp96 is essential for infection with vesicular stomatitis virus

Stuart Bloor, Jonathan Maelfait, Rebekka Krumbach, Rudi Beyaert, Felix Randow and Douglas T. Fearon
Proceedings of the National Academy of Sciences of the United States of America
Vol. 107, No. 15 (April 13, 2010), pp. 6970-6975
Stable URL: http://www.jstor.org/stable/25665287
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Endoplasmic reticulum chaperone gp96 is essential for infection with vesicular stomatitis virus
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Abstract

The envelope glycoprotein of vesicular stomatitis virus (VSV-G) enables viral entry into hosts as distant as insects and vertebrates. Because of its ability to support infection of most, if not all, human cell types VSV-G is used in viral vectors for gene therapy. However, neither the receptor nor any specific host factor for VSV-G has been identified. Here we demonstrate that infection with VSV and innate immunity via Toll-like receptors (TLRs) require a shared component, the endoplasmic reticulum chaperone gp96. Cells without gp96 or with catalytically inactive gp96 do not bind VSV-G. The ubiquitous expression of gp96 is therefore essential for the remarkably broad tropism of VSV-G. Cells deficient in gp96 also lack functional TLRs, which suggests that pathogen-driven pressure for TLR-mediated immunity maintains the broad host range of VSV-G by positively selecting for the ubiquitous expression of gp96.

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