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      Interplay between the cellular autophagy machinery and positive-stranded RNA viruses

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          Abstract

          Autophagy is a conserved cellular process that acts as a key regulator in maintaining cellular homeostasis. Recent studies implicate an important role for autophagy in infection and immunity by removing invading pathogens and through modulating innate and adaptive immune responses. However, several pathogens, notably some positive-stranded RNA viruses, have subverted autophagy to their own ends. In this review, we summarize the current understanding of how viruses with a positive-stranded RNA genome interact with the host autophagy machinery to control their replication and spread. We review the mechanisms underlying the induction of autophagy and discuss the pro- and anti-viral functions of autophagy and the potential mechanisms involved.

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          Selective autophagy mediated by autophagic adapter proteins.

          Terje Johansen, Trond Lamark (2011)
          Mounting evidence suggests that autophagy is a more selective process than originally anticipated. The discovery and characterization of autophagic adapters, like p62 and NBR1, has provided mechanistic insight into this process. p62 and NBR1 are both selectively degraded by autophagy and able to act as cargo receptors for degradation of ubiquitinated substrates. A direct interaction between these autophagic adapters and the autophagosomal marker protein LC3, mediated by a so-called LIR (LC3-interacting region) motif, their inherent ability to polymerize or aggregate as well as their ability to specifically recognize substrates are required for efficient selective autophagy. These three required features of autophagic cargo receptors are evolutionarily conserved and also employed in the yeast cytoplasm-to-vacuole targeting (Cvt) pathway and in the degradation of P granules in C. elegans. Here, we review the mechanistic basis of selective autophagy in mammalian cells discussing the degradation of misfolded proteins, p62 bodies, aggresomes, mitochondria and invading bacteria. The emerging picture of selective autophagy affecting the regulation of cell signaling with consequences for oxidative stress responses, tumorigenesis and innate immunity is also addressed.
          Article 0 comments Cited 306 times – based on 0 reviews     Review now
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            Lysosomes and autophagy in cell death control.

            Guido Kroemer, Marja Jäättelä (2005)
            Lysosomal hydrolases participate in the digestion of endocytosed and autophagocytosed material inside the lysosomal/autolysosomal compartment in acute cell death when released into the cytosol and in cancer progression following their release into the extracellular space. Lysosomal alterations are common in cancer cells. The increased expression and altered trafficking of lysosomal enzymes participates in tissue invasion, angiogenesis and sensitization to the lysosomal death pathway. But lysosomal heat-shock protein 70 locally prevents lysosomal-membrane permeabilization. Similarly, alterations in the autophagic compartment are linked to carcinogenesis and resistance to chemotherapy. Targeting these pathways might constitute a novel approach to cancer therapy.
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              Modification of intracellular membrane structures for virus replication

              Sven Miller, Jacomine Krijnse-Locker (2008)
              Key Points Plus-stranded RNA viruses induce large membrane structures that might support the replication of their genomes. Similarly, cytoplasmic replication of poxviruses (large DNA viruses) occurs in associated membranes. These membranes originate from the endoplasmic reticulum (ER) or endosomes. Membrane vesicles that support viral replication are induced by a number of RNA viruses. Similarly, the poxvirus replication site is surrounded by a double-membraned cisterna that is derived from the ER. Analogies to autophagy have been proposed since the finding that autophagy cellular processes involve the formation of double-membrane vesicles. However, molecular evidence to support this hypothesis is lacking. Membrane association of the viral replication complex is mediated by the presence of one or more viral proteins that contain sequences which associate with, or integrate into, membranes. Replication-competent membranes might contain viral or cellular proteins that contain amphipathic helices, which could mediate the membrane bending that is required to form spherical vesicles. Whereas poxvirus DNA replication occurs inside the ER-enclosed site, for most RNA viruses the topology of replication is not clear. Preliminary results for some RNA viruses suggest that their replication could also occur inside double-membrane vesicles. We speculate that cytoplasmic replication might occur inside sites that are 'enwrapped' by an ER-derived cisterna, and that these cisternae are open to the cytoplasm. Thus, RNA and DNA viruses could use a common mechanism for replication that involves membrane wrapping by cellular cisternal membranes. We propose that three-dimensional analyses using high-resolution electron-microscopy techniques could be useful for addressing this issue. High-throughput small-interfering-RNA screens should also shed light on molecular requirements for virus-induced membrane modifications.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Acta Biochim Biophys Sin (Shanghai)
                Journal ID (iso-abbrev): Acta Biochim. Biophys. Sin. (Shanghai)
                Journal ID (publisher-id): abbs
                Journal ID (hwp): abbs
                Title: Acta Biochimica et Biophysica Sinica
                Publisher: Oxford University Press
                ISSN (Print): 1672-9145
                ISSN (Electronic): 1745-7270
                Publication date (Print): May 2012
                Publication date (Electronic): 16 February 2012
                Volume: 44
                Issue: 5
                Pages: 375-384
                Affiliations
                Department of Pathology & Laboratory Medicine, UBC James Hogg Research Centre , Institute for Heart + Lung Health , St Paul's Hospital , University of British Columbia , Vancouver, BC V6Z 1Y6, Canada
                Author notes
                [* ]Correspondence address. Tel: +1-604-682-2344 ext. 62847; Fax: +1-604-806-9274; E-mail: honglin.luo@ 123456hli.ubc.ca
                Article
                Publisher ID: gms010
                DOI: 10.1093/abbs/gms010
                PMC ID: 7110239
                PubMed ID: 22343377
                SO-VID: 6245e62e-8a65-4265-8ae7-190e9f26ffed
                Copyright © © The Author 2012. Published by ABBS Editorial Office in association with Oxford University Press on behalf of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
                License:

                This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

                History
                Date received : 14 December 2011
                Date accepted : 13 January 2012
                Categories
                Subject: Review
                Subject: Editor's Choice

                Keywords: autophagy,positive-stranded rna viruses,autophagosome,p62/sqstm1,double-membrane vesicle,xenophagy
                Data availability:
                Keywords: autophagy, positive-stranded rna viruses, autophagosome, p62/sqstm1, double-membrane vesicle, xenophagy

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