A specific interaction between coat protein and helper component correlates with aphid transmission of a potyvirus

Virology. 1997 Apr 28;231(1):141-7. doi: 10.1006/viro.1997.8521.

Abstract

Specific binding between the coat protein (CP) and the helper component (HC) of the tobacco vein mottling potyvirus (TVMV) was characterized using a protein blotting-overlay protocol. In this in vitro assay, HC interacted with either virions or CP monomers originating from the aphid-transmissible TVMV-AT but not from the non-aphid-transmissible TVMV-NAT. There was a strong correlation between the aphid transmissibility of a series of TVMV variants having mutations in the DAG motif of the CP and their ability to bind HC. Expression of TVMV CP derivatives in bacteria allowed a precise determination of the minimum domain mediating HC binding. This domain is composed of seven amino acids, including the DAG motif (DTVDAGK), located in the N-terminus of the TVMV CP at amino acid positions 2 to 8.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aphids / virology
  • Capsid / metabolism*
  • Cysteine Endopeptidases / metabolism*
  • Insect Vectors / virology
  • Molecular Sequence Data
  • Plants, Toxic
  • Potyvirus / metabolism*
  • Protein Binding
  • Tobacco / virology
  • Viral Proteins / metabolism*

Substances

  • Viral Proteins
  • Cysteine Endopeptidases
  • HC-Pro protein, potyvirus