Ebolavirus VP35 interacts with the cytoplasmic dynein light chain 8

J Virol. 2009 Jul;83(13):6952-6. doi: 10.1128/JVI.00480-09. Epub 2009 Apr 29.

Abstract

The viral protein VP35 of ebolavirus (EBOV) is implicated to have diverse roles in the viral life cycle. We employed a yeast two-hybrid screen to search for VP35 binding partners and identified the cytoplasmic dynein light chain (DLC8) as a protein that interacts with VP35. Mapping analysis unraveled a consensus motif, SQTQT, within VP35 through which VP35 binds to DLC8. The disruption of DLC8 binding does not affect the ability of VP35 to inhibit type I IFN production. Given that VP35 from various EBOV species interacts with DLC8, this interaction may have a role in regulating the EBOV life cycle.

Publication types

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

MeSH terms

  • Amino Acid Motifs
  • Binding Sites
  • Cell Line
  • Cytoplasmic Dyneins
  • Dyneins / metabolism*
  • Ebolavirus / chemistry*
  • Humans
  • Nucleocapsid Proteins
  • Nucleoproteins / metabolism*
  • Protein Binding
  • Protein Interaction Mapping
  • Viral Core Proteins / metabolism*

Substances

  • Nucleocapsid Proteins
  • Nucleoproteins
  • Viral Core Proteins
  • nucleoprotein VP35, Ebola virus
  • DYNLL1 protein, human
  • Cytoplasmic Dyneins
  • Dyneins