The charged residues in the surface-exposed C-terminus of the Soybean mosaic virus coat protein are critical for cell-to-cell movement

Virology. 2013 Nov;446(1-2):95-101. doi: 10.1016/j.virol.2013.07.033. Epub 2013 Aug 25.

Abstract

The Soybean mosaic virus (SMV) coat protein (CP) is necessary for virion assembly and viral cell-to-cell and long-distance movements in plants. We previously showed that the C-terminal region of the SMV CP is required for CP self-interaction. In the present study, we generated SMV mutants containing CPs with single amino acid substitutions of the charged amino acids in the C-proximal region. Infectivity and cell-to-cell movement of the SMV mutants were examined in soybean plants. Through this genetic approach, we identified three charged amino acid residues (R245, H246, and D250) in the surface-exposed C-terminus of the SMV CP that are critical for virus cell-to-cell and long-distance movement. Our findings suggest that the identified charged amino acids in the surface-exposed C-terminus of SMV CP are critical for CP intersubunit interactions and thereby for cell-to-cell and long-distance movement and virion assembly.

Keywords: Coat protein; Movement; Potyvirus; SMV; Virion assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Amino Acids / genetics
  • Amino Acids / metabolism*
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism*
  • DNA Mutational Analysis
  • Glycine max / virology
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Potyvirus / genetics
  • Potyvirus / physiology*
  • Protein Conformation
  • Virus Internalization*
  • Virus Release*

Substances

  • Amino Acids
  • Capsid Proteins