Insights into the antiviral activity of phospholipases A2 (PLA2s) from snake venoms

Int J Biol Macromol. 2020 Dec 1:164:616-625. doi: 10.1016/j.ijbiomac.2020.07.178. Epub 2020 Jul 19.

Abstract

Viruses are associated with several human diseases that infect a large number of individuals, hence directly affecting global health and economy. Owing to the lack of efficient vaccines, antiviral therapy and emerging resistance strains, many viruses are considered as a potential threat to public health. Therefore, researches have been developed to identify new drug candidates for future treatments. Among them, antiviral research based on natural molecules is a promising approach. Phospholipases A2 (PLA2s) isolated from snake venom have shown significant antiviral activity against some viruses such as Dengue virus, Human Immunodeficiency virus, Hepatitis C virus and Yellow fever virus, and have emerged as an attractive alternative strategy for the development of novel antiviral therapy. Thus, this review provides an overview of remarkable findings involving PLA2s from snake venom that possess antiviral activity, and discusses the mechanisms of action mediated by PLA2s against different stages of virus replication cycle. Additionally, molecular docking simulations were performed by interacting between phospholipids from Dengue virus envelope and PLA2s from Bothrops asper snake venom. Studies on snake venom PLA2s highlight the potential use of these proteins for the development of broad-spectrum antiviral drugs.

Keywords: Antiviral drugs; Phospholipases A(2); Snake venom; Virus.

Publication types

  • Review

MeSH terms

  • Animals
  • Antiviral Agents / pharmacology*
  • Dengue Virus / drug effects
  • Drug Resistance, Viral / drug effects
  • HIV / drug effects
  • Hepacivirus / drug effects
  • Molecular Docking Simulation
  • Phospholipases A2 / pharmacology*
  • Reptilian Proteins / pharmacology
  • Snake Venoms / enzymology*
  • Snakes / metabolism*
  • Yellow fever virus / drug effects

Substances

  • Antiviral Agents
  • Reptilian Proteins
  • Snake Venoms
  • Phospholipases A2