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Home 2018

Antiviral Activities of Cu2+ Ions in Viral Prevention, Replication, RNA Degradation, and for Antiviral Efficacies of Lytic Virus, ROS-Mediated Virus, Copper Chelation

Author: Tsuneo Ishida, 99 (2018) 125-145

2024-05-22
Reading Time: 9 mins read
0

ABSTRACT

Copper has been known for decades that marked changes of micronutrient homeostasis in the host are accompanied by infection or inflammation. Copper levels in the serum are significantly elevated in response to inflammation that copper accumulates at sites of inflammation. Easily oxidized copper oxide nanoparticles (CuONPs) are widely used as catalysts that the ability of CuONPs to reduce bacterial population and virus application is enhanced. The mechanism of copper-mediated inactivation of herpes simplex virus (HSV) is by which cupric ions oxidatively damage biomolecules. Virus-mediated subjugation and modulation of host lipids during infection that the life cycle of most viruses proceeds through a series of basic steps: binding and internalization, fusion, uncoating, of the viral genome, its replication, assembly of new particles, and budding or release of the newly made viruses. The HIV-1 protein Vpu is an 81-amino-acid (16-kDa) type I which the presence of Vpu leads to the degradation of BST-2 via an endosome-lysosome degradation pathway. Oxidative degradation by a Cu-metalloenzyme, and ubiquitin-mediated degradation of cellular proteins were exploited. Copper can disrupt the lytic cycle of the Coccolithovirus. Lysins represent a novel class of anti-infectives derived from bacteriophage which lysins are bacterial cell wall hydrolytic enzymes that selectively and rapidly kill specific bacteria. Regarding copper induced cellular toxicity, several mechanisms have been proposed based on the formations of ROS by free Cu ions as cupric and cuprous ions can participate in redox reactions. ROS (O2ˉ,・OH, OHˉ), Cu+ and H2O2 play the important roles for viral inactivations. Thujaplicin-copper chelates inhibit influenza virus-induced apoptosis. Pyrrolidine dithiocarbamate as a metal ion binding agent inhibits the activity of the viral proteases of polyprotein processing and RNA replication of HRV. Chelation enables metals are capable of ligand scavenging via complexation, since reverse transcriptase enzyme inhibits the growth and replication of RNA tumor viruses. Thus, copper complex and copper chelation enhance antiviral efficacy.

 

References

  • Mario Manto. Abnormal Copper Homeostasis: Mechanisms and Roles in Neurodegeneration, Toxics, 2 (2014) 327-345.
  • Josko Osredkar and Natasa Sustar; Copper and Zinc, Biological Role and Significance of Copper/Zinc Imbalance, Journal of Clinical Toxicology, S3:001 (2011) p. 1-18
  • Amab Gupta and Svetlana; Human copper transporters: mechanism, role in human diseases and therapeutic potential, Future Med Chem. 1(6), September 1:(2009) 1125-1142.
  • Isidoros Iakovidis, Ioannis Delimaris, and Stylianos M. Piperakis: Copper and Its Complexes in Medicine: A Biochemical Approach, Molecular Biology International, 2011 (2011) 13 pages.
  • Nuria Verdaguer, Diego Ferrero and Mathur R.N. Murthy: Viruses and viral proteins, IUCrJ, 1 (2014) 492-504.
  • C. Chaturvedi, Richa Shrivastava and R.K. Upreti: Viral infections and trace elements: A complex interaction, Current Science, 87, No. 11 (2004) 1536-1554.
  • Ishida: Bacteriolysis of Cu2+ ion solution in bacterial cell walls/cell membrane and DNA base-pairing damage, Biomedical Research on Trace Element, 27(4) (2016) 151-161.
  • Ishida; Mechanism of Antibacterial Activities of Cu(II) Ions against Staphylococcus aureus and Escherichia coli on the Ground of Results Obtained from Dilution Medium Method, Virology & Immunology Journal, Vol. 1, Issue 3 (2017) 1-8 page.
  • Victoria Hodgkinson and Michael J.Petris: Copper Homeostasis at the Host-Pathogen Interface, Journal of Biological Chemistry, 287, April (2012) 13549-13555.
  • Murray Woodbury DVM, MSc, MSc: Copper Balance in Bison- Are you Bison Getting Enough ? Epidemiology, (2006) 1-6pages.
  • Richard A. Festa and Dennis J. Thiele: Copper: An essential metal in biology, Current Biology, 21, No. 21 (2011) 7 pages.
  • Bonnie Ransom, Marc Solioz, Daniel Krewski et al: Copper and human health: Biochemistry, genetics, and strategies for modelling dose-response relationships, Journal of Toxicology and Environmental Health, Parts B, 10 (2007) 157-222.
  • Maria Marjorette O. Pena, Ketth A. Koch, and Dennis J. Thiele: Dynamic regulation of copper uptake and detoxification genes in Saccharomyces cerevisiae, Molecular and Cellular Biology, 18, No. 5 (1998) 2514-2523.
  • Cissy X. Li, Julie E. Gleason, Sean X. Zhang, et al: Candida albicans adapts to host copper during infection by swapping metal cofactors for superoxide dismutase, PNAS, 8 (2015) E5336-E5343.
  • Uri Sheryn, Shilo Rosenwasser, Shifra Ben-Dor et al: Modulation of host ROS metabolism is essential for viral infection of a bloom-forming coccolithophore in the ocean, International Society for Microbial Ecology, 10 (2016) 1742-1754.
  • Angelique N. Besold, Edward M. Culbertson, and Valeria C. Culotta: The Yin and Yang of Copper During Infection, J Biol Inorg Chem. 21(2) (2016) 137-144.
  • Weiss, P.L. Carver: Role of divalent metals in infectious disease susceptibility and outcome, Clinical Microbiology and Infection, 24(2018)16-23.
  • Tegue Hari Sucipto, Siti Churrotin, Harsasi Setyawati et al: Antiviral activity of copper(II) chloride dihydrate against dengue virus type-2 in vero cell, Indonesian Journal of Tropical and Infectious Diseases, 6, No. 4 (2017) 84-89.
  • Borkow, R.W. Sidwell, D.F. Smee et al: Neutralizing viruses in suspensions by copper oxide-based filters, Antimicrobial Agents and Chemotherapy, 51, No. 7 (2007) 2605-2607.
  • Gadi Borkow, Humberto H. Lara, Chandice Y. Covington et al: Deactivation of HIV type 1 in medium by copper oxide-containing filters, Antimicrobial Agents and Chemotherapy, 52, No. 2 (2008) 518-525.
  • Borkow, S.S. Zhou, T. Page, J. Gabbay: A novel anti-influenza copper oxide containing respiratory face mask, PLOS ONE, 5, Issue 6 (2010) 1-9 pages.
  • Jose-Luis Sagripanti, Licia B. Routson, and C. David Lytle: Virus inactivation by copper or iron ions alone and in the presence of peroxide, Applied and Environmental Microbiology, 59, No.12 (1993) 4374-4376.
  • Ren, D. Hu, E.W.C. Cheng, et al. Characterisation of copper oxide nanoparticles for antimicrobial applications, International Journal of Antimicrobial Agents, 33 (2009) 587-590.
  • Mohammadyari, S.T. Razavipour, M. Mohammadbeigi et al: Explore in-vivo toxicity assessment of copper oxide nanoparticle in Wister rats, Journal of Biology and Today’s World, 3(6)(2014)124-128.
  • Lai, H. Zhao, Y. Zhang, K. Guo et al: Intranasal delivery of copper oxide nanoparticles induces pulmonary toxicity and fibrosis in C57BL/6 mice, Scientific Reports, 8 (2018) 1-10 pages
  • Fujimori, T. Sato, T. Hayata et al: Novel antiviral characteristics of nanosized copper(I) iodide particles showing inactivation activity against 2009 Pandemic H1N1 influenza virus, Applied and Environmental Microbiology, 78(4) (2011) 951-955.
  • J. Broglie, B. Alston, Chang Yang, et al: Antiviral activity of gold/copper sulfide core/shell nanoparticles against human norovirus virus-like particles, PLOS ONE,10 (10) (2015) 1-14.
  • Jonathan K. Pokorski and Nicole F. Steinmetz: The art of engineering viral nanoparticles, Mol Pharm., 8(1) (2011) 29-43.
  • -L. Sagripanti, L.B. Routson, A.C. Bonifacino, and C.D. Lytle: Mechanism of copper-mediated inactivation of HSV, Antimicrobial Agents and Chemotherapy, 41, No. 4 (1997) 812-817.
  • Sarah L. Warnes, C. William Keevil: Inactivation of norovirus on dry copper alloy surfaces, PLOS ONE, 8, issue 9 (2013) 1-9 page
  • O. Noyce, H. Michels, and C.W. Keevil: Inactivation of influenza A virus on copper versus stainless steel surfaces, Applied and Environmental Microbiology, 73, No. 8 (2007) 2748-2750.
  • Gregor Grass, Christopher Rensing, and Marc Solioz: Metallic copper as an antimicrobial surface, Applied and Environmental Microbiology, 77, No. 5 (2011) 1541-1547.
  • L. Warner and C.W. Keevil: Mechanism of copper surface toxicity in vancomycin-resistant enterococci following wet or dry surface contact, Applied and Environmental Microbiology, 77, No. 17 (2011) 6049-6059.
  • O’Gorman, H. Humphreys: Application of copper to prevent and control infection. Where are we now? Journal of Hospital Infection, XXX (2012) 1-7.
  • Prachayasittikul, S. Prachayasittikul, S. Ruchirawat, V. Prachayasittikul: 8-Hydroxyquinolines: a review of their metal chelating properties and medicinal applications, Drug Design, Development and Therapy, 7 (2013) 1157-1178.
  • Michela Mazzon and Jason Mercer: Lipid interactions during virus entry and infection, Cellular Microbiology, 16(10) (2014) 1493-1502.
  • Sierra-Aragon and Hauke Walter: Targets for inhibition of HIV replication: Entry, enzyme action, release and maturation, Intervirology, 55 (2012) 84-97.
  • Adam L. Feire, Heidi Koss, and Teresa Compton: Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain, PNAS, 101 (2004) 15470-15475.
  • Jiang He, Eileen Sun, Miriam V. Bujny et al: Dual function of CD81 in influenza virus uncoating and budding, PLOS Pathogen, 9, Issue 10 (2013) 1-15.
  • Subrata Barman and Debi P. Nayak: Lipid raft disruption by cholesterol depletion enhances influenza a virus budding from MDCK cells, Journal of Virology, 81, No. 22 (2007) 12169-12178.
  • A. Yondola, F. Fernandes, A. Belicha-Villanueva et al: Budding capability of the influenza virus neuraminidase can be modulated by tetherin, Journal of Virology, 85, No. 6 (2011) 2480-2491.
  • D. Mackenzie, N. J Foot, Sushma Anand, et al: Regulation of the divalent ion transporter via membrane budding, Cell Discovery, 2 (2016) 14 pages
  • Sideri, Y. Yashiroda, D.A. Ellis et al: The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants in Schizosaccharomyces pombe, Microbial Cell, 4, No. 1 (2016) 16-28.
  • Shishkov, T. Varadinova, M. Panteva, and P. Bontchev: Effect of complexes of zinc, cobalt and copper with d-aminosugars on the replication of herpes simplex virus type 1(HSV-1), Metal-Based Drugs, 4, No. 1 (1997) 35-38.
  • Miyamoto, Y. Kusagaya, N. Endoa, A. Sometani et al: Thujaplicin-copper chelates inhibit replication of human influenza viruses, Antiviral Research, 39(2) (1998) 89-100.
  • 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.
  • Cao, Y. Li, X. Jin, et al: Molecular mechanism of divalent-metal-induced activation of NS3 helicase and insights into Zica virus inhibitor design, Nucleic Acids Research, 44, No. 21 (2016) 10505-10514.
  • C. Rupp, M. Locatelli, A. Grieser et al: Host cell copper transporters CTR1 and ATP7A are important for influenza A virus replication, Virology Journal, Open Access, (2017) 12 pages.
  • Subramaniam, I. Vohra, A. lyer et al: A paradoxical relationship between Resveratrol and copper(II) with respect to degradation of DNA and RNA, F1000 Research 4 (2016) page 1-12.
  • S. Oxford and D.D. Perrin: Inhibition of particle-associeted RNA-dependent RNA polymerase activity of influenza viruses by chelating agents, J. Gen. Virol. 23 (1974) 59-71.
  • L. Douglas, K. Viswanathan, Matthew N. McCarroll et al: Vpu directs the degradation of the HIV virus restriction factor BST-2/Tetherin via a βTrCP-dependent mechanism, Journal of Virology, 83, No. 16 (2009) 7931-7947.
  • M. Gaglia, S. Covvarrubias, W. Wong and B. Glaunsinger: A common strategy for Host RNA Degradation by divergent viruses, Journal of virology, 86, No. 17 (2012) 9527-9530
  • Emma Abernathy and Britt Glaunsinger: Emerging role for RNA degradation in viral replication and antiviral defense, Virology, (2015) 600-608.
  • Sarah L. Warnes, Zoe R. Little, C. William Keevil: Human coronavirus 229E infectious on common touch surface materials, Asm. Org. 6, issue 6 (2015) 1-9.
  • L. Warnes, E.N. Summersgill, C. William Keevil: Inactivation of murine norovirus on a range of copper alloy surfaces is accompanied by loss of capsid integrity, aem. Applied and Environmetal Microbiology, 81, No. 3 (2015) 1085-1095
  • S. Manuel, M.D. Moore, L.A. Jaykus: Destruction of the capsid and genome of GII.4 human norovirus occurs during exposure to metal alloys containing copper, Applied and Environmental Microbiology, 81, No. 15 (2015) 4940-
  • Feng, D.N. Everly, Jr., and G.S. Read: mRNA decay during HSV infections: Protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A, Journal of Virology, 79, No. 15 (2005) 9651-9664.
  • Lora A. Shiflett, G. Sullivan Read: mRNA de cay during HSV infections: Mutations that affect translation of an mRNA influence the sites at which it is cleaved by the HSV virion host shutoff (Vhs) protein, Journal of Virology, 87, No. 1 (2013) 94-109.
  • D. Karousis, S. Nasif and O. Muhlemann: Nonsense-mediated mRNA decay: novel mechanistic insights and biological impact, Wiley Interdiscip Rev RNA, 7(5) (2016) 661-682.
  • Robert Hogg: Viral evasion and manipulation of host RNA quality control pathways, Journal of Virology, 90, No.16 (2019) 7010-7016.
  • Burgess, A. Pourchet, C.Hajdu, L. Chiriboga et al: Targeting poxvirus decapping enzymes and mRNA decay to generate an effective oncolytic virus, Molecular Therapy: Oncolytics, 8 (2018) 71-81.
  • J. Quinlan, M.D. Sweeney, L. Lo Leggio, et al: Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components, PNAS, 108, No. 37 (2011) 15079-15084.
  • Aaron Ciechanover and Alan L. Schwartz: Ubiquitin-mediated degradation of cellular proteins in health and diseases, SCIENCE FRONTIER, 35(1) (2008) 3-6
  • Gledhill, A. Devez, A. Highfield et al: Effect of metals on the lytic cycle of the Coccolithovirus, EhV86, frontier in MICROBIOROGY, 3 (2012) 1-10.
  • Pastagia, R. Schuch, V.A. Fischeth: Lysins: the arrival of pathogen-directed anti-infectives, Journal of Medical Microbiology, 62 (2013) 1506-1516.
  • E. Schmitz, R.Schuch, and V.A. Fischetti: Identifying active phage lysins through functional viral metagenomics, Applied and Environmental Microbiology, 76, No. 21 (2010) 7181-7187.
  • M. Dreher-Lesnick, J.E. Schreier and S. Stibitz: Development of phage lysin LysA2 for use in improved purity assays for live biotherapeutic products, Viruses, 7 (2015) 6675-6688.
  • Shu-Ming Kuo, Chi-Jene Chen, Shih-Cheng Chang et al: Inhibition of avian influenza A virus replication in human cells by host restriction factor TUFM is correlated with autophagy, American Society for Microbiology, 8, Issue 3 (2017) 1-18.
  • Mohammad Latif Reshi, Yi-Che Su, and Jiann-Ruey Hong: RNA virus: ROS-mediated cell death, International Journal of Cell Biology, 2014 (2014) 467-452.
  • Meunier, E. Strable, and M.G. Finn: Crosslinking of and coupling to viral capsid proteins by tyrosine oxidation, Chemistry & Biology, 11 (2004) 319-326.
  • Lin, R. Wang, W. X. 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 (2016) 1-16
  • Arun Srivastava: Antiviral activity of copper complexes of isoniazid against RNA tumor viruses, RESONANCE, (2009) 754-756.
  • Y. Yoo, J. Pradarelli, A. Haseley et al: Copper chelation enhances antitumor efficacy and systemic delivery of oncolytic HSV, Clinical Cancer Research, 18(18) (2012) 4931-4941.
  • S. Jarosz, A. Marek, Z. Gradzki, M. Kwiecien, B. Kaczmarek: The effect of feed supplementation with s copper-glycine chelate and copper sulphate on selected humoral and cell-mediated immune parameters, plasma superoxide dismutase activity, ceruloplasmin and cytokine concentration in broiler chickens, J Anim Physiol Anim Nutr. 102 (2017) e326-e335.
  • L. Hegde, P. Bharathi, A. Suram, et al: Challenges associated with metal chelation therapy in Alzheimer’s disease, J. Alzheimer’s disease, 17(3) (2010) 457-468.

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