Flavivirus NS5 associates with host-cell proteins zonula occludens-1 (ZO-1) and regulating synaptic membrane exocytosis-2 (RIMS2) via an internal PDZ binding mechanism

Biol Chem. 2009 Apr;390(4):319-23. doi: 10.1515/BC.2009.041.

Abstract

Dengue virus (DENV) and tick-borne encephalitis virus (TBEV) are flaviviruses, which can cause lethal hemorrhagic fever and encephalitis, respectively. Here, we demonstrate that the TBEV-NS5 and DENV-NS5 proteins use an internal binding mechanism to target human PDZ proteins. TBEV-NS5 has high affinity to regulating synaptic membrane exocytosis-2 (RIMS2) and Scribble, whereas DENV-NS5 binds primarily to the tight junction protein zonula occludens-1 (ZO-1). Targeting of TBEV-NS5 to the plasma membrane is stabilised by ZO-1; however, DENV-NS5 co-localises with ZO-1 in the nucleus. These interactions have potential important roles in the ability of flaviviruses to manipulate cell proliferation, junction permeability and the interferon pathways.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Dengue Virus*
  • Humans
  • Membrane Proteins / metabolism*
  • Membrane Transport Proteins / metabolism*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / metabolism*
  • PDZ Domains*
  • Phosphoproteins / metabolism*
  • Sequence Alignment
  • Synaptic Membranes / drug effects
  • Synaptic Membranes / virology*
  • Tight Junctions*
  • Viral Nonstructural Proteins / metabolism*
  • Viral Nonstructural Proteins / pharmacology
  • Zonula Occludens-1 Protein

Substances

  • Membrane Proteins
  • Membrane Transport Proteins
  • NS5 protein, flavivirus
  • Nerve Tissue Proteins
  • Phosphoproteins
  • RIMS3 protein, human
  • TJP1 protein, human
  • Viral Nonstructural Proteins
  • Zonula Occludens-1 Protein