A specific interaction between coat protein and helper component correlates with aphid transmission of a potyvirus.
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.
Blanc
S
S
Department of Plant Pathology, University of Kentucky, Lexington 40546, USA.
López-Moya
J J
JJ
Wang
R
R
García-Lampasona
S
S
Thornbury
D W
DW
Pirone
T P
TP
D000595:Amino Acid Sequence; D000818:Animals; D001042:Aphids / Q000821:virology; D002213:Capsid / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D007303:Insect Vectors / Q000821:virology; D008969:Molecular Sequence Data; D010947:Plants, Toxic; D017800:Potyvirus / Q000378:metabolism*; D011485:Protein Binding; D014026:Nicotiana / Q000821:virology; D014764:Viral Proteins / Q000378:metabolism*
D014764:Viral Proteins; D003546:Cysteine Endopeptidases; C072775:HC-Pro protein, potyvirus