S-nitrosylation of viral proteins

Molecular bases for antiviral effect of nitric oxide

Marco Colasanti, Tiziana Persichini, Giorgio Venturini, Paolo Ascenzi

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

Nitric oxide (NO) is considered an important signaling molecule implied in various different physiological processes, including nervous transmission, vascular regulation, and immune defence, as well as the pathogenesis of several diseases. NO reportedly also has an antiviral effect on several DNA and RNA virus families. The NO-mediated S-nitrosylation of vital and host (macro)molecules appears to be an intriguing general mechanism for the control of the virus life cycle. In this respect, NO is able to nitrosylate cysteine-containing enzymes (e.g., proteases, reverse transcriptase, and ribonucleotide reductase). Moreover, zinc-fingers and related domains present in enzymes (e.g., HIV-1-encoded integrase or herpes simplex virus type-1 heterotrimeric helicase-primase complex) or nucleocapsid proteins may be considered as NO targets. Also, NO may regulate both host (e.g., nuclear factor-κB) and vital-encoded (e.g., HIV-1 tat protein or Epstein-Bart virus Zta) transcriptional factors that are involved in virus replication. Finally, NO-mediated S-nitrosylation of cysteine-containing glycoproteins and hemagglutinin may also occur. Here, NO targets are summarised, and the molecular bases for the antiviral effect of NO are discussed.

Original languageEnglish
Pages (from-to)25-31
Number of pages7
JournalIUBMB Life
Volume48
Issue number1
DOIs
Publication statusPublished - 1999

Fingerprint

Viral Proteins
Antiviral Agents
Nitric Oxide
Viruses
Cysteine
Human Immunodeficiency Virus tat Gene Products
DNA Primase
tat Gene Products
Physiological Phenomena
Ribonucleotide Reductases
Nucleocapsid Proteins
Integrases
Molecules
DNA Viruses
RNA Viruses
RNA-Directed DNA Polymerase
Zinc Fingers
Hemagglutinins
Human Herpesvirus 1
Enzymes

Keywords

  • Antiviral agent
  • Nitric oxide
  • Virus replication

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Genetics
  • Molecular Biology

Cite this

S-nitrosylation of viral proteins : Molecular bases for antiviral effect of nitric oxide. / Colasanti, Marco; Persichini, Tiziana; Venturini, Giorgio; Ascenzi, Paolo.

In: IUBMB Life, Vol. 48, No. 1, 1999, p. 25-31.

Research output: Contribution to journalArticle

Colasanti, M, Persichini, T, Venturini, G & Ascenzi, P 1999, 'S-nitrosylation of viral proteins: Molecular bases for antiviral effect of nitric oxide', IUBMB Life, vol. 48, no. 1, pp. 25-31. https://doi.org/10.1080/152165499307387
Colasanti, Marco ; Persichini, Tiziana ; Venturini, Giorgio ; Ascenzi, Paolo. / S-nitrosylation of viral proteins : Molecular bases for antiviral effect of nitric oxide. In: IUBMB Life. 1999 ; Vol. 48, No. 1. pp. 25-31.
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