A Specific Interaction between Coat Protein and Helper Component Correlates with Aphid Transmission of a Potyvirus

• Published in: Virology (New York, N.Y.) N.Y.), 1997-04, Vol.231 (1), p.141-147
• Main Authors: Blanc, Stéphane, López-Moya, Juan-José, Wang, Renyuan, García-Lampasona, Sandra, Thornbury, David W., Pirone, Thomas P.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Aphids - virology; arthropod pests; Capsid - metabolism; Cysteine Endopeptidases - metabolism; Insect Vectors - virology; Life Sciences; Molecular Sequence Data; Nicotiana - virology; plant health; plant pests; plant viruses; Plants, Toxic; Potyvirus - metabolism; Protein Binding; Viral Proteins - metabolism
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1006/viro.1997.8521

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 thisin vitroassay, 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.