RNA binding property and RNA chaperone activity of dengue virus core protein and other viral RNA-interacting proteins

FEBS Lett. 2011 Aug 19;585(16):2575-81. doi: 10.1016/j.febslet.2011.06.038. Epub 2011 Jul 19.

Abstract

In this study we showed that the dengue virus (DENV) core protein forms a dimer with an α-helix-rich structure, binds RNA and facilitates the strand annealing process. To assess the RNA chaperone activity of this core protein and other dengue viral RNA-interacting proteins, such as NS3 helicase and NS5 proteins, we engineered cis- and trans-cleavage hammerhead ribozyme constructs carrying DENV genomic RNA elements. Our results indicate that DENV core protein facilitates typical hammerhead structure formation by acting as an RNA chaperone and DENV NS5 has a weak RNA chaperone activity, while DENV NS3 helicase failed to refold RNA with a complex secondary structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Dengue Virus*
  • Genome, Viral / genetics
  • Molecular Chaperones / metabolism*
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Engineering
  • RNA Helicases / metabolism
  • RNA, Catalytic / genetics
  • RNA, Viral / chemistry
  • RNA, Viral / genetics
  • RNA, Viral / metabolism*
  • Serine Endopeptidases / metabolism
  • Viral Core Proteins / metabolism*
  • Viral Nonstructural Proteins / metabolism

Substances

  • Molecular Chaperones
  • NS3 protein, flavivirus
  • RNA, Catalytic
  • RNA, Viral
  • Viral Core Proteins
  • Viral Nonstructural Proteins
  • hammerhead ribozyme
  • Serine Endopeptidases
  • RNA Helicases