Sensitivity of hepatitis C virus RNA to the antiviral enzyme ribonuclease L is determined by a subset of efficient cleavage sites

J Interferon Cytokine Res. 2004 Nov;24(11):664-76. doi: 10.1089/jir.2004.24.664.

Abstract

Ribonuclease L (RNase L) cleaves RNA predominantly at single-stranded UA and UU dinucleotides. Intriguingly, hepatitis C virus (HCV) RNAs have a paucity of UA and UU dinucleotides, and relatively interferon (IFN)-resistant strains have fewer UA and UU dinucleotides than do more IFN-sensitive strains. In this study, we found that contextual features of UA and UU dinucleotides dramatically affected the efficiency of RNase L cleavage in HCV RNA. HCV genotype la RNA was cleaved by RNase L into fragments 200-1000 bases in length, consistent with 10-50 RNase L cleavage sites within the 9650-base long viral RNA. Using primer extension, we found that HCV RNA structures with multiple single-stranded UA and UU dinucleotides were cleaved most efficiently by RNase L. UA and UU dinucleotides with 3' proximal C or G residues were cleaved infrequently, whereas UA and UU dinucleotides within dsRNA structures were not cleaved. 5'-GUAC-3' and 5'-CUUC-3' were particularly unfavorable contexts for cleavage by RNase L. More than 60% of the UA and UU dinucleotides in HCV la RNA were not cleaved by RNase L because of these contextual features. The 10-30 most efficiently cleaved sites were responsible for approximately 50%-85% of all RNase L cleavage events. Our data indicate that a relatively small number of the UA and UU dinucleotides in HCV RNA mediate the overall sensitivity of HCV RNA to cleavage by RNase L.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antiviral Agents / pharmacology*
  • Binding Sites
  • Cytoplasm / metabolism
  • DNA Primers / chemistry
  • Dose-Response Relationship, Drug
  • Endoribonucleases / chemistry
  • HeLa Cells
  • Hepacivirus / genetics*
  • Hepatitis C / drug therapy*
  • Humans
  • Nucleic Acid Conformation
  • Nucleotides / chemistry
  • Plasmids / metabolism
  • RNA / chemistry
  • RNA, Double-Stranded / chemistry
  • RNA, Messenger / metabolism
  • RNA, Viral*
  • Ribonucleases / pharmacology*
  • Temperature
  • Time Factors

Substances

  • Antiviral Agents
  • DNA Primers
  • Nucleotides
  • RNA, Double-Stranded
  • RNA, Messenger
  • RNA, Viral
  • RNA
  • Endoribonucleases
  • Ribonucleases
  • 2-5A-dependent ribonuclease