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2018 | 97 | 28-50
Article title

Antiviral Activities of Zn2+ Ions for Viral Prevention, Replication, Capsid Protein in Intracellular Proliferation of Viruses

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EN
In zinc homeostasis, zinc transporters ZIP and ZnT show tissue specificity and developmental and stimulus responsive expression patterns. The course of the life cycles of viral infections is governed by complex interactions between the virus and the host cellular system. Viruses depend on a host cell for their protein synthesis that the virus must first bind to the host cell, and then the virus enters in the cytoplasm which the genome is liberated from the protective capsid and, either in the nucleus or in the cytoplasm. The use of cellular zinc metalloproteases is effective for virus entry and coronavirus fusion. Molecular aspects of dengue virus genome uncoating and the fate of the capsid protein and RNA genome early during infection were investigated and found that capsid is degraded after viral internalization by the host ubiquitin-proteasome system. These results provide the first insights for antiviral intervention into dengue virus uncoating by Zn-binding degradation and enzyme inhibition of nucleocapsid, capsid protein, viral genome. AZPs inhibit virus DNA replication. Increasing the intracellular Zn2+ concentration with zinc-ionophores like pyrithione can efficiently impair the replication of a variety of RNA viruses, including poliovirus and influenza virus. ZAP is a host antiviral factor that specifically inhibit the replication of certain viruses, including HIV-1, Sindbis virus, and Ebola virus. ZAP specifically binds to the viral mRNA and recruits the cellular RNA degradation machinery to degrade the target RNA, while molecular mechanism by which ZAP inhibits target RNA expression and regulation of antiviral activity have been remained unclear. ROS as byproducts play an important role in cell signaling and regulate hormone action, growth factors, cytokines, transcription, apoptosis, iron transport, immunomodulation, and neuromodulation which many retroviruses, DNA and RNA viruses can cause cell death by generating oxidative stress in infected cells.
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97
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28-50
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  • Life and Environment Science Research Division, 2-3-6, Saido, Midoriku, Saitama City, Saitama Prefecture, 〒336-0907, Japan
References
  • [1] N. Zahi Gammoh and L. Rink, Zinc in infection and inflammation, Nutrients, 9 (2017) 1-25.
  • [2] M. Gupta, V.K. Mahajan, K.S. Mehta, and P.S. Chauhan, Zinc therapy in dermatology: a review, Dermatology Research and Practice, 2014 (2014) 11 page.
  • [3] Andrea Honscheid, Lothar Rink and Hajo Haase, T-Lymphocytes: A target for stimulatory and inhibitory effects of zinc ions, Endocrine Metabolic & Immune Disorders Drug Targets, 9, 2 (2009) 132-144.
  • [4] P. Tennsted, D. Peisker, C. Bottcher et al, Phytochelatin synthesis is essential for the detoxification of excess zinc and contributes significantly to the accumulation of zinc, American Society of Plant Biologist, 149 (2009) 938-948.
  • [5] N. Verdague, D. Ferrero, and M.R.N. Murthy, Viruses and viral proteins, IUCrJ, 1 (2014) 492-504.
  • [6] U.C. Chaturvedi, R.Shrivastava and R.K.Upreti, Viral infections and trace elements: A complex interaction, Current Science 87, 11 (2004) 1536-1551.
  • [7] T. Ishida, Bacteriolysis and Destruction of Bacterial Cell Wall by Zinc(Ⅱ) Ions on the Basis of the Results Obtained from Halo Antibacterial Tests for Metallic Salt Solutions, Open Access Journal of Microbiology & Biotechnology, Volume 2, Issue 2, 2017, pp1-8.
  • [8] T. Ishida: Antibacterial mechanism of bacteriolyses of bacterial cell walls by zinc(II) ion induced activations of PGN autolysins and DNA damages, Journal of Genes and Proteins, J (2017) 1-7pages.
  • [9] U.C. Chaturvedi and R. Shrivastava, Interaction of viral proteins with metal ions: role in maintaining the structure and functions of viruses, FEMS Immunology and Medical Microbiology 43 (2005) 105-114.
  • [10] M. Lazarczyk and M. Favre, Role of Zn2+ ions in host-virus interaction, American Society for Microbiology 82, 23 (2008) 11486-11494.
  • [11] The HIV Life Cycle, HIV Overview, Understanding HIV/AIDSinfo, 18 (2017) 1-4.
  • [12] Erwann Le Rouzic and Serge Benichou: The Vpr protein from HIV-1: distinct roles along the viral life cycle, Retroviology, 2 (2005) page 1-14
  • [13] Chang Wook Kim and Kyong-Mi Chang: Hepatitis C virus: virology and life cycle, Clinical and Molecular Hepatology, 19, No. 1, (2013) 17-25.
  • [14] Annette Martin and Stanley M Lemon: Hepatitis A virus: From discovery to vaccines, Hepatology, (2006) S164-S170.
  • [15] V. Gauss-Muller and Y. Kusov: Replication of a hepatitis A virus replicon detected by genetic recombination in vivo. Journal of General Virology, 83 (2002) 2183-2192.
  • [16] T. Antoine, Y.K. Mishra, J. Trigilio, V. Tiwari et al: Prophylactic, therapeutic and neutralizing effects of zinc oxide tetrapod structures against herpes simplex virus type-2 infection, Antiviral Res. 96 (3)(2012) 363-375.
  • [17] T.E. Antoine, S.R. Hadigal, A.M. Yakoub et al: Intravaginal zinc oxide tetrapod nanoparticles as novel immunnoprotective agents against genital herpes, The Journal of Immunology, (2016) 4566-4575.
  • [18] N. Duggal, D. Jaishankar, T.Yadavalli et al: Zinc oxide tetrapods inhibit herpes simple virus infection of cultured corneas, Molecular Vision, 23 (2017) 26-38.
  • [19] A. Rein, D.E. Ott, J. Mirro et al: Inactivation of murine leukemia virus by compounds that react with the zinc finger in the viral nucleocapsid protein, Journal of Virology, 70, No. 8 (1996) 4966-4972.
  • [20] R.J.Gorelick, W.Fu, T.D.Gagliadi et al: Characterization of the block in replication of nucleocapsid protein zinc finger mutants from moloney mureine leukemia virus, Journal of Virology, 73, No. 10 (1999) 8185-8195.
  • [21] J.Guo, T.Wu, J.Anderson et al: Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer, Journal of Virology, 74, No.19 (2000) 8980-8988.
  • [22] N. Lee, R.J. Gorelick, and K. Musier-Forsyth: Zinc finger-dependent HIV-1 nucleocapsid protein-TAR RNA interactions, Nucleic Acids Res. 2003 Aug 15; 31(16): 4847–4855.
  • [23] X. Guo, John-William N. Carroll, M.R. MacDonald et al: The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs, Journal of virology, 78, No. 23 (2004) 12781-12787.
  • [24] M.S. Boukvalova, Gregory A Prince, Jorge CG Blanco : Inactivation of respiratory syncytial virus by zinc finger reactive compounds, Virology Journal, 7(2010)1-10.
  • [25] Y. Zhu, G. Chen, F.Lv et al: Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spiced viral mRNAs for degradation, PNAS 108, No. 38 (2011) 15834-15839.
  • [26] L. Sun, F. Lv, X. Guo and G. Gao: Glycogen synthase kinase 3(GSK3) modulates antiviral activity of zinc-finger antiviral protein, Journal of Biological Chemistry, 287, No. 27 (2012) 22882-22888.
  • [27] Yifang Xuan, Ling Liu, Sheng Shen, Hongyu Deng and Guangxia Gao. Zinc finger antiviral protein inhibits murine gammaherpesvirus 68 M2 expression and regulates viral latency in cultured cells, Journal of Virology, 86, No. 22 (2012) 12431-12434.
  • [28] R. Mao, H. Nie, D. Cai et al: Inhibition of hepatitis B virus replication by the host zinc finger antiviral protein, PLOS Pathogens, 9, Issue 7 (2013) 1-18.
  • [29] Lukhovitskaya NI, Solovieva AD, Boddeti SK, Thaduri S, Solovyev AG, Savenkov EI. An RNA virus-encoded zinc-finger protein acts as a plant transcription factor and induces a regulator of cell size and proliferation in two tobacco species, The Plant Cell, 25 (2013) 960-973.
  • [30] M.M.H. Li, Z. Lau, P. Cheung et al: TRIM25 enhances the antiviral action of zinc-finger antiviral protein (ZAP), PLOS Pathogens, Jan.6 (2017) 1-25.
  • [31] Tracy L. Hartman, and Robert W. Buckheit Jr.: The continuing evolution of HIV-1 therapy: Identification and development of novel antiretroviral agents targeting viral and cellular targets, Molecular Biology International, 2012(2012)17 pages.
  • [32] H. Zhao, F. Granberg, L. Elfineh et al: Stategic attack on host cell gene expression during adenovirus infection, J Virol. 2003 Oct; 77(20): 11006–11015.
  • [33] Erick de Clercq. Molecular targets for antiviral agents, The Journal of Pharmacology and Experimental Therapeutics, 297, No.1 (2001) 1-10.
  • [34] Takashi Sera: Inhibition of virus DNA replication by artificial zinc finger proteins, Journal of Virology, 79, No. 4 (2005) 2614-2619.
  • [35] G.Kumel, S.Schrader, H.Zentgraf et al: The mechanism of the antiherpetic activity of zinc sulphate, Journal of General Virology, 71 (1990) 2989-2997.
  • [36] K. Briknarova, C.J. Thomas, J. York and J.H. Nunberg: Structure of a zinc-binding domain in the Junin Virus envelope glycoprotein, Journal of Biological Chemistry, 286, No. 2 (2011) 1528-1536.
  • [37] J.M.Phillips, T.Gallagher, Susan R.Weiss: Neurovirulent murine coronavirus JHM.SD use cellular zinc metalloproteases for virus entry and cell-cell fusion, Journal of Virology, 91, issue 8 (2017) 1-20.
  • [38] Joanne York and Jack H. Nunberg: A novel zinc-binding domain is essential for formation of the functional Junin virus envelope glycoprotein complex, Journal of Virology, 81, No. 24 (2007) 13385-13391.
  • [39] J. Corver, R. Bron, H. Snippe et al: Membrane fusion activity of semliki forest virus in a liposomal model system specific inhibition by Zn2+ ions, Virology, 238 (1997) 14-21.
  • [40] Catherine Y. Liu and Margaret Kielian: Identification of a specific region in the E1 fusion protein involved in zinc inhibition of semliki forest virus fusion, Journal of Virology, 86, No. 7 (2012) 3588-3594.
  • [41] Jean-Stephane Gatot, Isabelle Callebaut, Carine Van Lint et al: Brovine leukemia virus SU protein interacts with zinc, and mutations within two interacting regions differently affect viral fusion and infectivity in vivo, Journal of Virology, 76, No. 16 (2006) 7956-7967.
  • [42] Anne M. Haywood: Membrane uncoating of intact enveloped viruses, Journal of Virology, 84, No. 21 (2010) 10946-10955.
  • [43] L.A. Byk, N.G. Iglesias, F.A.De Maio et al: Dengue virus genome uncoating requires ubiquitination, American Society for Microbiology, 7, issue 3 (2016) 1-16.
  • [44] E.J. Firpo and E.L. Palma: Inhibition of food and mouth disease virus and procapsid synthesis by zinc ions, Archives of Virology, 61 (1979) 175-181.
  • [45] M.A. Tortorici, P.D. Ghiringhelli, M.E. Lozano et al: Zinc-binding properties of Junin virus nucleocapsid protein, Journal of General Virology, 82 (2001) 121-128.
  • [46] H.de Rocquigny, V. Shvadchak, S. Avilov et al: Targeting the viral nucleocapsid protein in anti-HIV-1 therapy, Medicinal Chemistry, 8 (2008) 24-35.
  • [47] R. Goila-Gaur, M.A.Khan, E. Miyagi et al: Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity, Retrovirology, 4 (2007) 1-10.
  • [48] Nele Matthes, Jeroen R.Mesters, Bruno Coutard et al: The non-structural protein Nsp10 of mouse hepatitis virus binds zinc ions and nucleic acids, FEBS Letters, 580 (2006) 4143-4149.
  • [49] Christine Elster, Eric Fourest, F. Baudin et al: A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction, Journal of General Virology, 75 (1994) 37-42.
  • [50] A.L.Anzellotti, Q.Liu, M.J.Bloemink, J.N.Scarsdale, and N.Farrell: Targeting retroviral Zn finger-DNA interactions: A small-molecule approach using the electrophilic nature of trans-platinum-nucleobase compounds, Chemistry & Biology, 13 (2006) 539-548.
  • [51] Thomas J Cradick, Kathy Keck, Shannon Bradshaw et al: Zinc-finger nucleases as a novel therapeutic strategy for targeting hepatitis B virus DNAs, Molecular Therapy, 18 (2010) 947-954.
  • [52] Moshe Bracha and Milton J. Schlesinger: Inhibition of Sindbis virus replication by zinc ions, Virology, 72, issue1 (1976) 272-277.
  • [53] Eric Ka-Wai Hui, Katherine Ralston, Amrit K.Judd and Debi P.Nayak: Conserved cysteine and histidine residues in the putative zinc finger motif of the influenza A virus M1 protein are not critical for influenza virus replication, Journal of General Virology, 84 (2003) 3105-3113.
  • [54] Rahaman O. Suhara and James E. Crowe, Jr.: Effect of zinc salts on respiratory syn- cytial virus replication, Antimicrobial Agents and Chemotherapy, 48, No. 3 (2004) 783-790.
  • [55] B.M. Krenn, B. Holzer, E. Gaudernak, A. Triendl et al: Inhibition of polyprotein processing and RNA replication of human rhinovirus by pyrrolidine dithiocarbamate involves metal ions, Journal of Virology, 79, No. 22 (2005) 13892-13899.
  • [56] A.J.W.te Velthuis, S.H.E. van den Worm, Amy C.Sims et al: Zn2+ inhibits coronavirus and arterivirus RNA polymerase activity in Vitro and zinc ionophores block the replication of these viruses in cell culture, PLOS Pathogens, 6, issue 11 (2010) 1-10.
  • [57] Katherine J. Fenstermacher and Jeffrey J.DeStefano: Mechanism of HIV reverse transcriptase inhibition by zinc, Journal of Biological Chemistry, 286, No. 25 (2011) 40433-40442.
  • [58] Inge Erk, Jean-Claude Huet, Mariela Duarte et al: A zinc ion controls assembly and stability of the major capsid protein of rotavirus, Journal of Virology, 77, No. 6 (2003) 3595-3601.
  • [59] Haitham Sobhy: A review of functional motifs utilized by viruses, Proteomes, 4(3) (2016) 1-21 pages.
  • [60] J.A. Turpin, S.J. Terpening, C.A. Schaeffer et al: Inhibitors of HIV type 1 zinc fingers prevent normal processing of gag precursors and result in the release of noninfectious virus particles, Journal of Virology, 70, No. 9 (1996) 6180-6189.
  • [61] Stephen P. Goff: Retrovirus restriction factors, Molecular Cell, 16 (2004) 849-859.
  • [62] Ana Beloso, Concepcion Martinnez, Juan Valcarcel et al: Degradation of cellular mRNA during influenza virus infection: its possible role in protein synthesis shutoff, Journal of General Virology, 73 (1992) 575-581.
  • [63] Yiping Zhu and Guangxio Gao: ZAP-mediated mRNA degradation, RNA Biology, 5, issue 2 (2008) 65-67.
  • [64] Jonathan Houseley and David Tollervey: The many pathways of RNA degradation, Cell, 136 (2009) 763-776.
  • [65] F.T.Vreede, A.Y. Chan, J.Sharps, E.Fodor: Mechanisms and functional implications of the degradation of host RNA polymeraseⅡin influenza virus infected cells, Virology, 396 (2010) 125-134.
  • [66] Yiping Zhu, Guifang Chen, Fengxiang Lv, Xinlu Wang et al: Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation, PNAS, 108, No. 38 (2011) 15834-15839.
  • [67] W.Hou, Q.Tian, J.Zheng, and H.L.Bonkovsky: Zinc mesoporphyrin induces rapid proteasomal degradation of hepatitis C nonstructural 5A protein in human hepatoma cells, Gastroenterology, 138 (2010) 1909-1919.
  • [68] Xiaojiao Zheng, Xinlu Wang, Fan Tu et al: TRIM25 is required for the antiviral activity of zinc finger antiviral protein, Journal of Virology, 91, issue 9 (2017) 1-17.
  • [69] T.Kozaki, M.Takahama, T.Misawa et al: Role of zinc-finger anti-viral protein in host defense against Sindbis virus, International Immunology, 27, No. 7 (2015) 357-364.
  • [70] Emma Abernathy and Britt Glaunsinger: Emerging roles for RNA degradation in viral replication and antiviral defense, HHS Public Access, Virology, (2016)1-13.
  • [71] Emma Abernathy, Britt Gaunsinger: Emerging roles for RNA degradation in viral replication and antiviral defense, Virology, 479-480 (2015) 600-608.
  • [72] Mohammad Latif Reshi, Yi-Che Su, and Jiann-Ruey Hong: RNA viruses: ROS-mediated cell death, International Journal of Cell Biology, 2014 (2014) 16 pages
  • [73] S. A Lozano-Sepulveda, O. L Bryan-Marrugo, C.Cordova-Fletes et al: Oxidative stress modulation in hepatitis C virus infected cells, World Journal of Hepatology, 7 (29) (2015) 2880-2889.
  • [74] L.Suwanprinya, N.P.Morales, P.Sanvarinda et al: Dengue virus-induced reactive oxygen species production in rat microglial cells, Jpn. J. Infect. Dis. 70 (2017) 383-387.
  • [75] Xian Lin, Ruifang Wang, Wei Zou et al: The influenza virus H5N1 infection can induce ROS production for viral replication and host cell death in A549 cells modulated by human Cu/Zn superoxide dismutase (SOD1) overexpression, Viruses, 8 (2015) 1-16.
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bwmeta1.element.psjd-8ab246c3-8e3f-4707-b97f-0c14fa91b094
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