Ebola virus VP35 interaction with dynein LC8 regulates viral RNA synthesis

J Virol. 2015 May;89(9):5148-53. doi: 10.1128/JVI.03652-14. Epub 2015 Mar 4.

Abstract

Ebola virus VP35 inhibits alpha/beta interferon production and functions as a viral polymerase cofactor. Previously, the 8-kDa cytoplasmic dynein light chain (LC8) was demonstrated to interact with VP35, but the functional consequences were unclear. Here we demonstrate that the interaction is direct and of high affinity and that binding stabilizes the VP35 N-terminal oligomerization domain and enhances viral RNA synthesis. Mutational analysis demonstrates that VP35 interaction is required for the functional effects of LC8.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cytoplasmic Dyneins / metabolism*
  • DNA Mutational Analysis
  • Ebolavirus / genetics
  • Ebolavirus / physiology*
  • Host-Pathogen Interactions*
  • Protein Binding
  • Protein Interaction Mapping*
  • RNA, Viral / biosynthesis*
  • Viral Regulatory and Accessory Proteins / genetics
  • Viral Regulatory and Accessory Proteins / metabolism*
  • Virus Replication*

Substances

  • RNA, Viral
  • VP35 protein, filovirus
  • Viral Regulatory and Accessory Proteins
  • DYNLL1 protein, human
  • Cytoplasmic Dyneins