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Importance of the C-terminal domain of soybean mosaic virus coat protein for subunit interactions

¹ Department of Agricultural Biotechnology and Center for Plant Molecular Genetics and Breeding Research, Seoul National University, Seoul 151-742, Korea
² National Institute of Agricultural Science and Technology, Rural Development Administration, Suwon 441-707, Korea

Correspondence
Kook-Hyung Kim
kookkim{at}snu.ac.kr

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.

Supplementary material is available in JGV Online.

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