Special Issue "Viruses and the Unfolded Protein Response"

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Animal Viruses".

Deadline for manuscript submissions: 1 December 2019.

Special Issue Editors

Dr. Craig McCormick
Guest Editor
Department of Microbiology and Immunology, Dalhousie University, Sir Charles Tupper Medical Building, Room 7-P 5850 College Street, Halifax, Nova Scotia, Canada B3H 4R2
Interests: influenza A virus; Kaposi’s sarcoma-associated herpesvirus; viral oncogenes; mRNA turnover and translation; stress granules; p-bodies; autophagy; unfolded protein response; inflammation; host shutoff
Special Issues and Collections in MDPI journals
Dr. Carolina Arias
E-Mail Website
Guest Editor
University of California Santa Barbara
Interests: herpesviruses; zika virus; protein synthesis; unfolded protein response; RNA-seq; CRISPR

Special Issue Information

Dear Colleagues,

Viruses use host cell translation machinery to synthesize viral proteins, and the endoplasmic reticulum (ER) to ensure proper folding, post-translational modification, and trafficking of transmembrane and secreted viral proteins. Overloading the ER’s folding capacity activates the unfolded protein response (UPR), whereby the ER stress sensors PERK, IRE1, and ATF6 initiate signals that transiently attenuate translation and stimulate the production of stress-mitigating transcription factors. UPR transcription increases production of ER protein folding machinery, expands the ER’s surface area, and increases degradation of misfolded proteins by ER-associated degradation (ERAD). The UPR also plays important roles in cell fate decisions and immune responses. At present, relatively little is known about how viruses manipulate the UPR and the functional consequences of these interactions.

For this Special Issue of Viruses, we hope to assemble a collection of research papers and reviews that provide a comprehensive view of this emerging field of virus research. Topics of interest include, but are not limited to:

  1. viral protein synthesis and interplay with the UPR and/or the integrated stress response;
  2. viral modulation of UPR sensors;
  3. viral modulation of UPR transcription;
  4. viral control of ERAD;
  5. effects of viral infection on UPR-dependent cell differentiation and cell fate;
  6. the UPR and viral pathogenesis; and
  7. therapeutic targeting of the UPR during viral infection.

We hope that this Special Issue will serve as a valuable resource to new and established researchers in the field, and frame important unanswered questions to focus future research efforts.

Dr. Craig McCormick
Dr. Carolina Arias
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


  • virus
  • protein
  • translation
  • endoplasmic reticulum
  • unfolded protein response
  • IRE1
  • XBP1
  • PERK
  • ATF6
  • ERAD
  • secretion

Published Papers (1 paper)

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Open AccessArticle
The Porcine Deltacoronavirus Replication Organelle Comprises Double-Membrane Vesicles and Zippered Endoplasmic Reticulum with Double-Membrane Spherules
Viruses 2019, 11(11), 1030; https://doi.org/10.3390/v11111030 - 05 Nov 2019
Porcine deltacoronavirus (PDCoV) was first identified in Hong Kong in 2012 from samples taken from pigs in 2009. PDCoV was subsequently identified in the USA in 2014 in pigs with a history of severe diarrhea. The virus has now been detected in pigs [...] Read more.
Porcine deltacoronavirus (PDCoV) was first identified in Hong Kong in 2012 from samples taken from pigs in 2009. PDCoV was subsequently identified in the USA in 2014 in pigs with a history of severe diarrhea. The virus has now been detected in pigs in several countries around the world. Following the development of tissue culture adapted strains of PDCoV, it is now possible to address questions regarding virus–host cell interactions for this genera of coronavirus. Here, we presented a detailed study of PDCoV-induced replication organelles. All positive-strand RNA viruses induce the rearrangement of cellular membranes during virus replication to support viral RNA synthesis, forming the replication organelle. Replication organelles for the Alpha-, Beta-, and Gammacoronavirus genera have been characterized. All coronavirus genera induced the formation of double-membrane vesicles (DMVs). In addition, Alpha- and Betacoronaviruses induce the formation of convoluted membranes, while Gammacoronaviruses induce the formation of zippered endoplasmic reticulum (ER) with tethered double-membrane spherules. However, the structures induced by Deltacoronaviruses, particularly the presence of convoluted membranes or double-membrane spherules, are unknown. Initially, the dynamics of PDCoV strain OH-FD22 replication were assessed with the onset of viral RNA synthesis, protein synthesis, and progeny particle release determined. Subsequently, virus-induced membrane rearrangements were identified in infected cells by electron microscopy. As has been observed for all other coronaviruses studied to date, PDCoV replication was found to induce the formation of double-membrane vesicles. Significantly, however, PDCoV replication was also found to induce the formation of regions of zippered endoplasmic reticulum, small associated tethered vesicles, and double-membrane spherules. These structures strongly resemble the replication organelle induced by avian Gammacoronavirus infectious bronchitis virus. Full article
(This article belongs to the Special Issue Viruses and the Unfolded Protein Response)
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