Mosquito La protein binds to the 3' untranslated region of the positive and negative polarity dengue virus RNAs and relocates to the cytoplasm of infected cells

Virology. 2007 Jan 5;357(1):29-40. doi: 10.1016/j.virol.2006.07.042. Epub 2006 Sep 7.

Abstract

The untranslated regions (UTRs) of the positive and negative strand RNAs of several viruses are major binding sites for cellular and viral proteins. Human La autoantigen is one of the cellular proteins that interacts with various positive strand RNA viral genomes including that of dengue virus (DEN) within the 5'- and 3'-UTRs of positive (+) and the 3'-UTR of negative strand (-) RNA, and with the nonstructural proteins NS3 and NS5, that form DEN replicase complex. Since DEN replicates in human and mosquito cells, some functional interactions have to be conserved in both hosts. In the present report, we demonstrate that mosquito La protein interacts with the 3'-UTRs of (+) and (-) polarity viral RNAs. The localization of La protein, examined by confocal microscopy, indicates that La protein is redistributed in DEN-infected cells. Furthermore, the presence of La protein in an in vitro replication system inhibited RNA synthesis in a dose-dependent manner, suggesting that La protein plays an important role in dengue virus replicative cycle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3' Untranslated Regions / metabolism*
  • Aedes
  • Animals
  • Autoantigens / metabolism*
  • Cell Line
  • Dengue Virus / physiology*
  • Insect Proteins / metabolism*
  • Nucleic Acid Conformation
  • Protein Binding
  • RNA, Viral / chemistry
  • RNA, Viral / metabolism*
  • Virus Replication

Substances

  • 3' Untranslated Regions
  • Autoantigens
  • Insect Proteins
  • RNA, Viral