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Viruses 2016, 8(9), 255; doi:10.3390/v8090255

Arms Race between Enveloped Viruses and the Host ERAD Machinery

Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA
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Author to whom correspondence should be addressed.
Academic Editor: Jaquelin Dudley
Received: 20 July 2016 / Revised: 12 September 2016 / Accepted: 12 September 2016 / Published: 19 September 2016
(This article belongs to the Special Issue Viruses, ERAD, and the Proteasome)
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Abstract

Enveloped viruses represent a significant category of pathogens that cause serious diseases in animals. These viruses express envelope glycoproteins that are singularly important during the infection of host cells by mediating fusion between the viral envelope and host cell membranes. Despite low homology at protein levels, three classes of viral fusion proteins have, as of yet, been identified based on structural similarities. Their incorporation into viral particles is dependent upon their proper sub-cellular localization after being expressed and folded properly in the endoplasmic reticulum (ER). However, viral protein expression can cause stress in the ER, and host cells respond to alleviate the ER stress in the form of the unfolded protein response (UPR); the effects of which have been observed to potentiate or inhibit viral infection. One important arm of UPR is to elevate the capacity of the ER-associated protein degradation (ERAD) pathway, which is comprised of host quality control machinery that ensures proper protein folding. In this review, we provide relevant details regarding viral envelope glycoproteins, UPR, ERAD, and their interactions in host cells. View Full-Text
Keywords: enveloped viruses; viral glycoproteins; endoplasmic reticulum-associated degradation; ERAD; unfolded protein response; UPR; ER stress enveloped viruses; viral glycoproteins; endoplasmic reticulum-associated degradation; ERAD; unfolded protein response; UPR; ER stress
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Frabutt, D.A.; Zheng, Y.-H. Arms Race between Enveloped Viruses and the Host ERAD Machinery. Viruses 2016, 8, 255.

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