Importance of the C-terminal domain of Soybean mosaic virus coat protein for subunit interactions
2006
Kang, S.H. | Lim, W.S. | Hwang, S.H. | Park, J.W. | Choi, H.S. | Kim, K.H.
The potyvirus coat protein (CP) is involved in aphid transmission, cell-to-cell movement and virus assembly, not only by binding to viral RNA, but also by self-interaction or interactions with other factors. In this study, a number of CP mutants of Soybean mosaic virus (SMV) containing deletions and site-directed mutations were generated and cloned into yeast two-hybrid vectors. Interaction was confirmed by the expression of reporter genes, including HIS3, ADE2 and MEL1, in yeast strain AH109. Deletion of the C-terminal region of the CP caused loss of the CP-CP self-interaction ability detected in CP mutants with the C-terminal region. Alanine substitution at the amino acid positions R190, E191, E212, R245, H246 and R249 disrupted CP-CP interaction, whereas substitutions at the amino acid positions R188, D189, D198, K205, K218 and D250 did not. These results indicate that the C-terminal region of SMV CP may contain a domain(s) or amino acids required for CP-CP interaction and virus assembly.
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