Review
Version 1
NOT YET PEER-REVIEWED
Arms Race between Enveloped Viruses and the Host ERAD Machinery
Version 1
: Received: 3 August 2016 / Approved: 4 August 2016 / Online: 4 August 2016 (11:44:59 CEST)
A peer-reviewed article of this Preprint also exists.
Frabutt, D.A.; Zheng, Y.-H. Arms Race between Enveloped Viruses and the Host ERAD Machinery. Viruses 2016, 8, 255. Frabutt, D.A.; Zheng, Y.-H. Arms Race between Enveloped Viruses and the Host ERAD Machinery. Viruses 2016, 8, 255.
Journal reference: Viruses 2016, 8, 255
DOI: 10.3390/v8090255
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 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 potentiating or inhibiting 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.
Subject Areas
enveloped viruses; viral glycoproteins; endoplasmic reticulum-associated degradation; ERAD; unfolded protein response; UPR; ER stress
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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