A Specific Interaction between Coat Protein and Helper Component Correlates with Aphid Transmission of a Potyvirus
| Autor: | Renyuan Wang, Sandra García-Lampasona, Thomas P. Pirone, David W. Thornbury, Stéphane Blanc, Juan José López-Moya |
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| Rok vydání: | 1997 |
| Předmět: |
0106 biological sciences
Molecular Sequence Data Potyvirus Coat protein 01 natural sciences 03 medical and health sciences Viral Proteins Capsid Virology Tobacco Animals Amino Acid Sequence 030304 developmental biology chemistry.chemical_classification 0303 health sciences Aphid biology A protein biology.organism_classification 3. Good health Amino acid Insect Vectors Cysteine Endopeptidases Plants Toxic chemistry Biochemistry Aphids Bacteria 010606 plant biology & botany Protein Binding |
| Zdroj: | Virology. 231(1):141-147 |
| ISSN: | 0042-6822 |
| DOI: | 10.1006/viro.1997.8521 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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