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      Virus Escape and Manipulation of Cellular Nonsense-Mediated mRNA Decay

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          Abstract

          Nonsense-mediated mRNA decay (NMD), a cellular RNA turnover pathway targeting RNAs with features resulting in aberrant translation termination, has recently been found to restrict the replication of positive-stranded RNA ((+)RNA) viruses. As for every other antiviral immune system, there is also evidence of viruses interfering with and modulating NMD to their own advantage. This review will discuss our current understanding of why and how NMD targets viral RNAs, and elaborate counter-defense strategies viruses utilize to escape NMD.

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          Nonsense-mediated mRNA decay: an intricate machinery that shapes transcriptomes.

          Søren Lykke-Andersen, Torben Heick Jensen (2015)
          Nonsense-mediated mRNA decay (NMD) is probably the best characterized eukaryotic RNA degradation pathway. Through intricate steps, a set of NMD factors recognize and degrade mRNAs with translation termination codons that are positioned in abnormal contexts. However, NMD is not only part of a general cellular quality control system that prevents the production of aberrant proteins. Mammalian cells also depend on NMD to dynamically adjust their transcriptomes and their proteomes to varying physiological conditions. In this Review, we discuss how NMD targets mRNAs, the types of mRNAs that are targeted, and the roles of NMD in cellular stress, differentiation and maturation processes.
          Article 0 comments Cited 348 times – based on 0 reviews     Review now
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            Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics.

            Lynne Maquat (2004)
            Studies of nonsense-mediated mRNA decay in mammalian cells have proffered unforeseen insights into changes in mRNA-protein interactions throughout the lifetime of an mRNA. Remarkably, mRNA acquires a complex of proteins at each exon-exon junction during pre-mRNA splicing that influences the subsequent steps of mRNA translation and nonsense-mediated mRNA decay. Complex-loaded mRNA is thought to undergo a pioneer round of translation when still bound by cap-binding proteins CBP80 and CBP20 and poly(A)-binding protein 2. The acquisition and loss of mRNA-associated proteins accompanies the transition from the pioneer round to subsequent rounds of translation, and from translational competence to substrate for nonsense-mediated mRNA decay.
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              Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon.

              M Shu, J Lykke, J Steitz (2000)
              Nonsense-mediated decay (NMD) rids eukaryotic cells of aberrant mRNAs containing premature termination codons. These are discriminated from true termination codons by downstream cis-elements, such as exon-exon junctions. We describe three novel human proteins involved in NMD, hUpf2, hUpf3a, and hUpf3b. While in HeLa cell extracts these proteins are complexed with hUpf1, in intact cells hUpf3a and hUpf3b are nucleocytoplasmic shuttling proteins, hUpf2 is perinuclear, and hUpf1 cytoplasmic. hUpf3a and hUpf3b associate selectively with spliced beta-globin mRNA in vivo, and tethering of any hUpf protein to the 3'UTR of beta-globin mRNA elicits NMD. These data suggest that assembly of a dynamic hUpf complex initiates in the nucleus at mRNA exon-exon junctions and triggers NMD in the cytoplasm when recognized downstream of a translation termination site.
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                Author and article information

                Contributors
                Robert Hogg: Role: Academic Editor
                Karen L. Beemon: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Viruses
                Journal ID (iso-abbrev): Viruses
                Journal ID (publisher-id): viruses
                Title: Viruses
                Publisher: MDPI
                ISSN (Electronic): 1999-4915
                Publication date (Electronic): 23 January 2017
                Publication date Collection: January 2017
                Volume: 9
                Issue: 1
                Electronic Location Identifier: 24
                Affiliations
                [1 ]Department of Biosciences, University of Helsinki, Helsinki FIN-00014, Finland
                [2 ]Department of Chemistry and Biochemistry, University of Bern, Bern CH-3012, Switzerland; claudia.bognanni@ 123456dcb.unibe.ch
                [3 ]Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern CH-3012, Switzerland
                Author notes
                [* ]Correspondence: giuseppe.balistreri@ 123456helsinki.fi (G.B.); oliver.muehlemann@ 123456dcb.unibe.ch (O.M.); Tel.: +358-294159550 (G.B.); +41-31-631-4627 (O.M.)
                Article
                Publisher ID: viruses-09-00024
                DOI: 10.3390/v9010024
                PMC ID: 5294993
                PubMed ID: 28124995
                SO-VID: 9fb86764-8faa-495c-96e8-c1ed324cb2dc
                Copyright © © 2017 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 18 November 2016
                Date accepted : 13 January 2017
                Categories
                Subject: Review

                ScienceOpen disciplines: Microbiology & Virology
                Keywords: rna quality control,gene expression,translation,rna-protein interactions
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology
                Keywords: rna quality control, gene expression, translation, rna-protein interactions

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