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      Relevance of signaling molecules for apoptosis induction on influenza A virus replication

      review-article
      Author(s): a , b , b , *
      Publication date (Electronic):
      Journal: Biochemical and Biophysical Research Communications
      Publisher: Elsevier
      Keywords: Akt, v-akt murine thymoma viral oncogene homolog 1, Apaf-1, apoptotic protease activating factor 1, Bax, Bcl-2-associated x protein, Bcl-2, B-cell lymphoma 2, BH, Bcl-2 homology, Caspases, cysteine–aspartic acid protease, DAP3, death-associated protein 3, DR4, death receptor 4, DR5, death receptor 5, FADD, Fas-associated death domain, IAV, influenza A virus, IFN, interferon, IPS-1, INF-β promoter stimulator protein 1, IRF3, IFN regulatory factor 3, JNK, c-Jun amino-terminal kinase, M, matrix protein, NF-κB, nuclear factor-κB, NA, neuraminidase, NP, nucleoprotein, NS1, non-structural protein 1, PI3K, phosphatidylinositol-3 kinase, RIG-I, retinoic acid-inducible gene-I, TNF-α, tumor necrosis factor α, TNFαR1, TNF-α receptor 1, TRADD, tumor necrosis factor receptor type 1-associated death domain protein, TRAIL, TNF-related apoptosis inducing ligand, XIAP, X-linked inhibitor of apoptosis protein, ZAPS, zinc finger antiviral protein, short form, Influenza A virus, Apoptosis, Signal transduction

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          Highlights

          • •

            Apoptosis is an important mechanism to maintain homeostasis.

          • •

            Infection of influenza A virus induces apoptosis in the virus infected cells.

          • •

            A large number of signaling molecules are involved in regulation of apoptosis.

          • •

            Functions of apoptosis related molecules are modulated by the viral proteins.

          • •

            Influenza A virus utilizes apoptosis signal molecules for effective propagation.

          Abstract

          Apoptosis is an important mechanism to maintain homeostasis in mammals, and disruption of the apoptosis regulation mechanism triggers a range of diseases, such as cancer, autoimmune diseases, and developmental disorders. The severity of influenza A virus (IAV) infection is also closely related to dysfunction of apoptosis regulation. In the virus infected cells, the functions of various host cellular molecules involved in regulation of induction of apoptosis are modulated by IAV proteins to enable effective virus replication. The modulation of the intracellular signaling pathway inducing apoptosis by the IAV infection also affects extracellular mechanisms controlling apoptosis, and triggers abnormal host responses related to the disease severity of IAV infections. This review focuses on apoptosis related molecules involved in IAV replication and pathogenicity, the strategy of the virus propagation through the regulation of apoptosis is also discussed.

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          Most cited references34

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          RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates.

          Andreas Pichlmair, Oliver Schulz, Choon Ping Tan … (2006)
          Double-stranded RNA (dsRNA) produced during viral replication is believed to be the critical trigger for activation of antiviral immunity mediated by the RNA helicase enzymes retinoic acid-inducible gene I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5). We showed that influenza A virus infection does not generate dsRNA and that RIG-I is activated by viral genomic single-stranded RNA (ssRNA) bearing 5'-phosphates. This is blocked by the influenza protein nonstructured protein 1 (NS1), which is found in a complex with RIG-I in infected cells. These results identify RIG-I as a ssRNA sensor and potential target of viral immune evasion and suggest that its ability to sense 5'-phosphorylated RNA evolved in the innate immune system as a means of discriminating between self and nonself.
          Article 0 comments Cited 663 times – based on 0 reviews     Review now
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            Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis.

            D Nicholson, A. Ali, N A Thornberry … (1995)
            The protease responsible for the cleavage of poly(ADP-ribose) polymerase and necessary for apoptosis has been purified and characterized. This enzyme, named apopain, is composed of two subunits of relative molecular mass (M(r)) 17K and 12K that are derived from a common proenzyme identified as CPP32. This proenzyme is related to interleukin-1 beta-converting enzyme (ICE) and CED-3, the product of a gene required for programmed cell death in Caenorhabditis elegans. A potent peptide aldehyde inhibitor has been developed and shown to prevent apoptotic events in vitro, suggesting that apopain/CPP32 is important for the initiation of apoptotic cell death.
            Article 0 comments Cited 514 times – based on 0 reviews     Review now
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              Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3.

              Hua Zou, William Henzel, Xuesong Liu … (1997)
              We report here the purification and cDNA cloning of Apaf-1, a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3. The NH2-terminal 85 amino acids of Apaf-1 show 21% identity and 53% similarity to the NH2-terminal prodomain of the Caenorhabditis elegans caspase, CED-3. This is followed by 320 amino acids that show 22% identity and 48% similarity to CED-4, a protein that is believed to initiate apoptosis in C. elegans. The COOH-terminal region of Apaf-1 comprises multiple WD repeats, which are proposed to mediate protein-protein interactions. Cytochrome c binds to Apaf-1, an event that may trigger the activation of caspase-3, leading to apoptosis.
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                Author and article information

                Contributors
                Tadaaki Miyazaki
                Journal
                Journal ID (nlm-ta): Biochem Biophys Res Commun
                Journal ID (iso-abbrev): Biochem. Biophys. Res. Commun
                Title: Biochemical and Biophysical Research Communications
                Publisher: Elsevier
                ISSN (Print): 0006-291X
                ISSN (Electronic): 1090-2104
                Publication date PMC-release: 28 October 2013
                Publication date (Print): 22 November 2013
                Publication date (Electronic): 28 October 2013
                Volume: 441
                Issue: 3
                Pages: 531-537
                Affiliations
                [a ]Aureo Science Co., Ltd., North 21, West 12, Kita-Ku, Sapporo, Hokkaido 001-0021, Japan
                [b ]Department of Probiotics Immunology, Institute for Genetic Medicine, Hokkaido University, North 15, West 7, Kita-Ku, Sapporo, Hokkaido 060-0815, Japan
                Author notes
                [* ]Corresponding author. Address: Department of Probiotics Immunology, Institute for Genetic Medicine, Hokkaido University, North 15, West 7, Kita-Ku, Sapporo, Hokkaido 060-0815, Japan. Fax: +81 11 706 8095. miyazaki@ 123456pop.med.hokudai.ac.jp miyazaki@ 123456czc.hokudai.ac.jp
                Article
                Publisher ID: S0006-291X(13)01781-6
                DOI: 10.1016/j.bbrc.2013.10.100
                PMC ID: 7092955
                PubMed ID: 24177013
                SO-VID: e282acf6-f15f-4333-ac96-09e8743036ca
                Copyright statement: Copyright © 2013 Elsevier Inc. All rights reserved.
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

                History
                Date received : 3 October 2013
                Categories
                Subject: Article

                ScienceOpen disciplines: Biochemistry
                Keywords: akt, v-akt murine thymoma viral oncogene homolog 1,apaf-1, apoptotic protease activating factor 1,bax, bcl-2-associated x protein,bcl-2, b-cell lymphoma 2,bh, bcl-2 homology,caspases, cysteine–aspartic acid protease,dap3, death-associated protein 3,dr4, death receptor 4,dr5, death receptor 5,fadd, fas-associated death domain,iav, influenza a virus,ifn, interferon,ips-1, inf-β promoter stimulator protein 1,irf3, ifn regulatory factor 3,jnk, c-jun amino-terminal kinase,m, matrix protein,nf-κb, nuclear factor-κb,na, neuraminidase,np, nucleoprotein,ns1, non-structural protein 1,pi3k, phosphatidylinositol-3 kinase,rig-i, retinoic acid-inducible gene-i,tnf-α, tumor necrosis factor α,tnfαr1, tnf-α receptor 1,tradd, tumor necrosis factor receptor type 1-associated death domain protein,trail, tnf-related apoptosis inducing ligand,xiap, x-linked inhibitor of apoptosis protein,zaps, zinc finger antiviral protein, short form,influenza a virus,apoptosis,signal transduction
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: akt, v-akt murine thymoma viral oncogene homolog 1, apaf-1, apoptotic protease activating factor 1, bax, bcl-2-associated x protein, bcl-2, b-cell lymphoma 2, bh, bcl-2 homology, caspases, cysteine–aspartic acid protease, dap3, death-associated protein 3, dr4, death receptor 4, dr5, death receptor 5, fadd, fas-associated death domain, iav, influenza a virus, ifn, interferon, ips-1, inf-β promoter stimulator protein 1, irf3, ifn regulatory factor 3, jnk, c-jun amino-terminal kinase, m, matrix protein, nf-κb, nuclear factor-κb, na, neuraminidase, np, nucleoprotein, ns1, non-structural protein 1, pi3k, phosphatidylinositol-3 kinase, rig-i, retinoic acid-inducible gene-i, tnf-α, tumor necrosis factor α, tnfαr1, tnf-α receptor 1, tradd, tumor necrosis factor receptor type 1-associated death domain protein, trail, tnf-related apoptosis inducing ligand, xiap, x-linked inhibitor of apoptosis protein, zaps, zinc finger antiviral protein, short form, influenza a virus, apoptosis, signal transduction

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