The secretory pathway and the actomyosin motility system are required for plasmodesmatal localization of the P7-1 of rice black-streaked dwarf virus

Arch Virol. 2013 May;158(5):1055-64. doi: 10.1007/s00705-012-1585-3. Epub 2012 Dec 28.

Abstract

Rice black-streaked dwarf virus (RBSDV), a plant-infecting reovirus (genus Fijivirus), generally induces virus-containing tubules in infected cells. The nonstructural protein P7-1, encoded by the first open reading frame of segment 7, is involved in forming the structural matrix of these tubules. In experiments to investigate the subcellular localization of P7-1 in Nicotiana benthamiana epidermal cells, fluorescence of P7-1:eGFP was observed in the nucleus, cytoplasm and cell periphery, and in punctate points along the cell wall of plasmolyzed cells. Co-localization with plasmodesmata-located protein 1 showed that P7-1 formed the punctate points at plasmodesmata. Mutational analysis demonstrated that transmembrane domain 1 and adjacent residues were necessary and sufficient for P7-1 to form punctate structures at the cell wall in the plasmolyzed cells. Chemical drug and protein inhibitor treatments indicated that P7-1 utilized the ER-to-Golgi secretory pathway and the actomyosin motility system for its intracellular transport. The plasmodesmatal localization of RBSDV P7-1 is therefore dependent on the secretory pathway and the actomyosin motility system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actomyosin / metabolism*
  • Artificial Gene Fusion
  • Genes, Reporter
  • Green Fluorescent Proteins / analysis
  • Green Fluorescent Proteins / genetics
  • Host-Pathogen Interactions*
  • Nicotiana / virology
  • Plasmodesmata / chemistry
  • Plasmodesmata / virology*
  • Recombinant Fusion Proteins / analysis
  • Recombinant Fusion Proteins / genetics
  • Reoviridae / pathogenicity*
  • Secretory Pathway*
  • Staining and Labeling / methods
  • Viral Nonstructural Proteins / metabolism*

Substances

  • Recombinant Fusion Proteins
  • Viral Nonstructural Proteins
  • enhanced green fluorescent protein
  • Green Fluorescent Proteins
  • Actomyosin