The complex subcellular distribution of satellite panicum mosaic virus capsid protein reflects its multifunctional role during infection

Virology. 2008 Jun 20;376(1):154-64. doi: 10.1016/j.virol.2008.03.013. Epub 2008 Apr 28.

Abstract

Satellite panicum mosaic virus (SPMV) depends on its helper Panicum mosaic virus for replication and movement in host plants. The positive-sense single-stranded genomic RNA of SPMV encodes a 17-kDa capsid protein (CP) to form 16-nm virions. We determined that SPMV CP accumulates in both cytosolic and non-cytosolic fractions, but cytosolic accumulation of SPMV CP is exclusively associated with virions. An N-terminal arginine-rich motif (N-ARM) on SPMV CP is used to bind its cognate RNA and to form virus particles. Intriguingly, virion formation is dispensable for successful systemic SPMV RNA accumulation, yet this process still depends on an intact N-ARM. In addition, a C-terminal domain on the SPMV CP is necessary for self-interaction. Biochemical fractionation and fluorescent microscopy of green fluorescent protein-tagged SPMV CP demonstrated that the non-cytosolic SPMV CP is associated with the cell wall, the nucleus and other membranous organelles. To our knowledge, this is the first report that a satellite virus CP not only accumulates exclusively as virions in the cytosol but also is directed to the nucleolus and membranes. That SPMV CP is found both in the nucleus and the cell wall suggests its involvement in viral nuclear import and cell-to-cell transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsid Proteins / metabolism*
  • Cell Membrane / chemistry
  • Cell Nucleus / chemistry
  • Cell Wall / chemistry
  • Cytosol / chemistry*
  • Panicum / virology*
  • Protein Binding
  • Protein Interaction Mapping
  • Protein Structure, Tertiary
  • RNA, Viral / metabolism
  • Satellite Viruses / physiology*
  • Tombusviridae / physiology*
  • Virion / chemistry
  • Virus Assembly / genetics

Substances

  • Capsid Proteins
  • RNA, Viral