Rice black-streaked dwarf virus P10 induces membranous structures at the ER and elicits the unfolded protein response in Nicotiana benthamiana

Virology. 2013 Dec;447(1-2):131-9. doi: 10.1016/j.virol.2013.09.001. Epub 2013 Sep 24.

Abstract

Endoplasmic reticular (ER) membrane modifications play an important role in viral RNA replication and virion assembly but little is known about the involvement of ER-membrane remodeling in the infection cycle of fijiviruses in plant cells. The subcellular localization of Rice black-streaked dwarf virus outer capsid P10 was therefore examined using live-cell imaging. P10 fused to eGFP formed vesicular structures associated with ER membranes in Nicotiana benthamiana epidermal cells and in rice protoplasts. Subcellular fractionation experiments confirmed that P10 is an integral membrane protein. Three predicted transmembrane domains and two less-well-defined domains were each able to target eGFP to the ER. Disruption of the actin cytoskeleton with LatB, indicated that the maintenance of P10-induced membrane structures required the intact actin cytoskeleton. P10 induced the expression of ER stress marker genes, including ER stress-related chaperones and transcription factor, indicating that RBSDV P10 triggers ER stress and the unfolded protein response.

Keywords: Capsid protein P10; ER membrane modification; ER stress; Rice black-streaked dwarf virus; Unfolded protein response.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Artificial Gene Fusion
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism*
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum / virology*
  • Genes, Reporter
  • Green Fluorescent Proteins / analysis
  • Green Fluorescent Proteins / genetics
  • Host-Pathogen Interactions*
  • Nicotiana / virology
  • Oryza / virology
  • Recombinant Fusion Proteins / analysis
  • Recombinant Fusion Proteins / genetics
  • Reoviridae / physiology*
  • Unfolded Protein Response*

Substances

  • Capsid Proteins
  • Recombinant Fusion Proteins
  • enhanced green fluorescent protein
  • Green Fluorescent Proteins