Selective inhibition of the West Nile virus methyltransferase by nucleoside analogs

Antiviral Res. 2013 Mar;97(3):232-9. doi: 10.1016/j.antiviral.2012.12.012. Epub 2012 Dec 22.

Abstract

The flavivirus methyltransferase (MTase) sequentially methylates the N-7 and 2'-O positions of the viral RNA cap (GpppA-RNA→m(7)GpppA-RNA→m(7)GpppAm-RNA), using S-adenosyl-l-methionine (SAM) as a methyl donor. We report here the synthesis and biological evaluation of a series of novel nucleoside analogs. Two of these compounds can effectively and competitively inhibit the WNV MTase with IC50 values in micromolar range and, more importantly, do not inhibit human MTase. The compounds can also suppress the WNV replication in cell culture.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Down-Regulation
  • Humans
  • Methyltransferases / antagonists & inhibitors*
  • Methyltransferases / genetics
  • Methyltransferases / metabolism
  • Nucleosides / chemical synthesis
  • Nucleosides / pharmacology*
  • Viral Proteins / antagonists & inhibitors*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism
  • Virus Replication / drug effects
  • West Nile Fever / virology*
  • West Nile virus / drug effects
  • West Nile virus / enzymology*
  • West Nile virus / genetics
  • West Nile virus / physiology

Substances

  • Nucleosides
  • Viral Proteins
  • Methyltransferases