Interaction of viral proteins with metal ions: role in maintaining the structure and functions of viruses
Open Access
- 1 February 2005
- journal article
- review article
- Published by Oxford University Press (OUP) in FEMS Immunology & Medical Microbiology
- Vol. 43 (2), 105-114
- https://doi.org/10.1016/j.femsim.2004.11.004
Abstract
Metal ions are integral part of some viral proteins and play an important role in their survival and pathogenesis. Zinc, magnesium and copper are the commonest metal ion that binds with viral proteins. Metal ions participate in maturation of genomic RNA, activation and catalytic mechanisms, reverse transcription, initial integration process and protection of newly synthesized DNA, inhibition of proton translocation (M2 protein), minus- and plus-strand transfer, enhance nucleic acid annealing, activation of transcription, integration of viral DNA into specific sites and act as a chaperone of nucleic acid. Metal ions are also required for nucleocapsid protein-transactivation response (TAR)–RNA interactions. In certain situations more than one metal ion is required e.g. RNA cleavage by RNase H. This review underscores the importance of metal ions in the survival and pathogenesis of a large group of viruses and studies on structural basis for metal binding should prove useful in the early design and development of viral inhibitors.Keywords
This publication has 65 references indexed in Scilit:
- Emerging themes in rotavirus cell entry, genome organization, transcription and replicationVirus Research, 2004
- Conserved cysteine and histidine residues in the putative zinc finger motif of the influenza A virus M1 protein are not critical for influenza virus replicationJournal of General Virology, 2003
- Leporipoxvirus Cu,Zn-Superoxide Dismutase (SOD) Homologs Are Catalytically Inert Decoy Proteins That Bind Copper Chaperone for SODPublished by Elsevier BV ,2003
- Differing Roles of the N- and C-terminal Zinc Fingers in Human Immunodeficiency Virus Nucleocapsid Protein-enhanced Nucleic Acid AnnealingPublished by Elsevier BV ,2003
- Effects of chromium on the immune systemFEMS Immunology & Medical Microbiology, 2002
- Models for protein–zinc ion binding sites. II. The catalytic sites*International Journal of Quantum Chemistry, 2001
- The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanismJournal of Molecular Biology, 1999
- Specific interactions of Cu2+ ions with fragments of envelope protein of hepatitis B virusJournal of Inorganic Biochemistry, 1996
- A Zinc Binding Site in Viral Serine ProteinasesBiochemistry, 1996
- ZINC PROTEINS: Enzymes, Storage Proteins, Transcription Factors, and Replication ProteinsAnnual Review of Biochemistry, 1992