Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
7.3
3.8
Journals
Viruses
Special Issues
Viruses and the OAS-RNase L Pathway
share announcement

Viruses and the OAS-RNase L Pathway

A special issue of Viruses (ISSN 1999-4915).

Deadline for manuscript submissions: closed (30 September 2019) | Viewed by 18624

Special Issue Editors

Prof. Dr. Susan Weiss

E-Mail Website
Guest Editor
Department of Microbiology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA
Interests: coronavirus pathogenesis; murine coronavirus; human respiratory coronaviruses; MERS-CoV; SARS-CoV-2; common CoVs; viral antagonism of innate immunity; OAS/RNase L; endogenous dsRNA induced pathogenesis; Zika virus
Prof. Dr. Robert H. Silverman

E-Mail Website
Guest Editor
Department of Cancer Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, USA

Special Issue Information

Dear Colleagues,

OAS-RNase L is a potent interferon-regulated antiviral pathway that severely limits the pathogenesis of many different types of viruses. Upon sensing viral (non-self) dsRNA, OASs produce 2’,5’-oligoadenylates (2-5A) that bind to and cause the activation of RNase L. RNase L then cleaves both the host and viral single-stranded RNA, thereby limiting protein production, virus replication and spread, and causing apoptosis. Recent and exciting advances emphasize the importance of OAS-RNase L in antiviral innate immunity. Some of these studies reveal how viruses evolved many strategies to antagonize OAS-RNase L, including sequestering dsRNA from OAS, degrading 2-5A by viral- or host-encoded enzymes or directly inhibiting RNase L. Other studies extend beyond the antiviral state into cellular responses to host (self) dsRNA induced by genetic or epigenetic events. This unique and first-of-its-kind issue on OAS-RNase L will contribute to our understanding of how this remarkable innate immune pathway impacts human health in the context of viral and genetic diseases and cancer.

Prof. Dr. Susan Weiss
Prof. Dr. Robert H. Silverman
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 submissions that pass pre-check are 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 2600 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.

Keywords

  • Ribonuclease L
  • oligoadenylate synthetase
  • 2’,5’-oligoadenylates
  • viral antagonists
  • phosphodiesterases
  • endogenous dsRNA
  • antiviral pathways

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (4 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

11 pages, 2908 KiB  
Communication
ABCE1 Acts as a Positive Regulator of Exogenous RNA Decay
by Takuto Nogimori, Koichi Ogami, Yuka Oishi, Ryoya Goda, Nao Hosoda, Yoshiaki Kitamura, Yukio Kitade and Shin-ichi Hoshino
Viruses 2020, 12(2), 174; https://doi.org/10.3390/v12020174 - 4 Feb 2020
Cited by 6 | Viewed by 4289
Abstract
The 2′-5′-oligoadenylate synthetase (OAS)/RNase L system protects hosts against pathogenic viruses through cleavage of the exogenous single-stranded RNA. In this system, an evolutionally conserved RNA quality control factor Dom34 (known as Pelota (Pelo) in higher eukaryotes) forms a surveillance complex with RNase L [...] Read more.
The 2′-5′-oligoadenylate synthetase (OAS)/RNase L system protects hosts against pathogenic viruses through cleavage of the exogenous single-stranded RNA. In this system, an evolutionally conserved RNA quality control factor Dom34 (known as Pelota (Pelo) in higher eukaryotes) forms a surveillance complex with RNase L to recognize and eliminate the exogenous RNA in a manner dependent on translation. Here, we newly identified that ATP-binding cassette sub-family E member 1 (ABCE1), which is also known as RNase L inhibitor (RLI), is involved in the regulation of exogenous RNA decay. ABCE1 directly binds to form a complex with RNase L and accelerates RNase L dimer formation in the absence of 2′-5′ oligoadenylates (2-5A). Depletion of ABCE1 represses 2-5A-induced RNase L activation and stabilizes exogenous RNA to a level comparable to that seen in RNase L depletion. The increased half-life of the RNA by the single depletion of either protein is not significantly affected by the double depletion of both proteins, suggesting that RNase L and ABCE1 act together to eliminate exogenous RNA. Our results indicate that ABCE1 functions as a positive regulator of exogenous RNA decay rather than an inhibitor of RNase L. Full article
(This article belongs to the Special Issue Viruses and the OAS-RNase L Pathway)
►▼ Show Figures

Graphical abstract

16 pages, 1894 KiB  
Article
Characteristics of Human OAS1 Isoform Proteins
by Han Di, Husni Elbahesh and Margo A. Brinton
Viruses 2020, 12(2), 152; https://doi.org/10.3390/v12020152 - 29 Jan 2020
Cited by 10 | Viewed by 4850
Abstract
The human OAS1 (hOAS1) gene produces multiple possible isoforms due to alternative splicing events and sequence variation among individuals, some of which affect splicing. The unique C-terminal sequences of the hOAS1 isoforms could differentially affect synthetase activity, protein stability, protein partner interactions and/or [...] Read more.
The human OAS1 (hOAS1) gene produces multiple possible isoforms due to alternative splicing events and sequence variation among individuals, some of which affect splicing. The unique C-terminal sequences of the hOAS1 isoforms could differentially affect synthetase activity, protein stability, protein partner interactions and/or cellular localization. Recombinant p41, p42, p44, p46, p48, p49 and p52 hOAS1 isoform proteins expressed in bacteria were each able to synthesize trimer and higher order 2′-5′ linked oligoadenylates in vitro in response to poly(I:C). The p42, p44, p46, p48 and p52 isoform proteins were each able to induce RNase-mediated rRNA cleavage in response to poly(I:C) when overexpressed in HEK293 cells. The expressed levels of the p42 and p46 isoform proteins were higher than those of the other isoforms, suggesting increased stability in mammalian cells. In a yeast two-hybrid screen, Fibrillin1 (FBN1) was identified as a binding partner for hOAS1 p42 isoform, and Supervillin (SVIL) as a binding partner for the p44 isoform. The p44-SVIL interaction was supported by co-immunoprecipitation data from mammalian cells. The data suggest that the unique C-terminal regions of hOAS1 isoforms may mediate the recruitment of different partners, alternative functional capacities and/or different cellular localization. Full article
(This article belongs to the Special Issue Viruses and the OAS-RNase L Pathway)
►▼ Show Figures

Figure 1

10 pages, 2538 KiB  
Article
RNase L Is Involved in Liposaccharide-Induced Lung Inflammation
by Ruhan Wei, Guanmin Chen, Naseh Algehainy, Chun Zeng, Chunfang Liu, Hongli Liu, Wendy Liu, Dennis Stacey and Aimin Zhou
Viruses 2020, 12(1), 73; https://doi.org/10.3390/v12010073 - 7 Jan 2020
Cited by 4 | Viewed by 3203
Abstract
RNase L mediates interferon (IFN) function during viral infection and cell proliferation. Furthermore, the role of RNase L in the regulation of gene expression, cell apoptosis, autophagy, and innate immunity has been well established in the last decade. Tissue distribution reveals that RNase [...] Read more.
RNase L mediates interferon (IFN) function during viral infection and cell proliferation. Furthermore, the role of RNase L in the regulation of gene expression, cell apoptosis, autophagy, and innate immunity has been well established in the last decade. Tissue distribution reveals that RNase L is highly expressed in the lung and other organs. However, the physiological roles of RNase L in the lung are largely unknown. In this study, we found that polysaccharide (LPS)-induced acute lung injury (ALI) was remarkably intensified in mice deficient in RNase L compared to wild type mice under the same condition. Furthermore, we found that RNase L mediated the TLR4 signaling pathway, and regulated the expression of various pro- and anti-inflammatory genes in the lung tissue and blood. Most importantly, RNase L function in macrophages during LPS stimulation may be independent of the 2-5A system. These findings demonstrate a novel role of RNase L in the immune response via an atypical molecular mechanism. Full article
(This article belongs to the Special Issue Viruses and the OAS-RNase L Pathway)
►▼ Show Figures

Figure 1

19 pages, 3851 KiB  
Article
The Cellular Localization of the p42 and p46 Oligoadenylate Synthetase 1 Isoforms and Their Impact on Mitochondrial Respiration
by Stig Skrivergaard, Monica Skou Jensen, Tine Breckling Rolander, Tram Bao Ngoc Nguyen, Amanda Bundgaard, Lene N. Nejsum and Pia M. Martensen
Viruses 2019, 11(12), 1122; https://doi.org/10.3390/v11121122 - 4 Dec 2019
Cited by 12 | Viewed by 4716
Abstract
The importance of the IFN-induced oligoadenylate synthetase (OAS) proteins and the OAS/RNase L pathway in the innate response against viral pathogens is well-established, however the observed differences in anti-viral activity between the human OAS1 p46 and p42 isoforms are not fully understood. The [...] Read more.
The importance of the IFN-induced oligoadenylate synthetase (OAS) proteins and the OAS/RNase L pathway in the innate response against viral pathogens is well-established, however the observed differences in anti-viral activity between the human OAS1 p46 and p42 isoforms are not fully understood. The protein expression of these isoforms is determined by the SNP rs10774671, either being an A or a G allele resulting in expression of either the p42 or the p46 isoform. Using fluorescence microscopy and immunoblot analysis of fractionated cell samples, we show here that the CaaX motif is of key importance to the cellular localization. The OAS1 p42 isoform is mainly located in the cytosol, whereas the p46 isoform with a C-terminal CaaX motif is translocated to membranous organelles, like the mitochondria. We furthermore observed differences between p42 and p46 in their effect on mitochondrial physiology using high resolution respirometry and fluorometry. Overexpression of OAS1 p42 and IFN-β treatment of HeLa cells (AA genotype) resulted in significantly increased respiration, which was not seen with p46 overexpression. The difference in subcellular localization and mitochondrial effect of these two OAS1 isoforms might help to explain the anti-viral mechanisms that differentiate these proteins. Full article
(This article belongs to the Special Issue Viruses and the OAS-RNase L Pathway)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-4
Back to TopTop