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The central and C-terminal domains of VPg of Clover yellow vein virus are important for VPg–HCPro and VPg–VPg interactions

¹ Pathogen Plant Interactions Group, Plant Breeding Science, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan
² Plant Genetic Engineering Laboratory, Biotechnology Institute, Akita Prefectural University, Ogata, Akita 010-0444, Japan

Correspondence
Ichiro Uyeda
uyeda{at}res.agr.hokudai.ac.jp

Interactions between the major proteins of Clover yellow vein virus (ClYVV) were investigated using a GAL4 transcription activator-based yeast two-hybrid system (YTHS). Self-interactions manifested by VPg and HCPro and an interaction between NIb and NIaPro were observed in ClYVV. In addition, a strong HCPro–VPg interaction was detected by both YTHS and by in vitro far-Western blot analysis in ClYVV. A potyvirus HCPro–VPg interaction has not been reported previously. Using YTHS, domains in ClYVV for the VPg self-interaction and the HCPro–VPg interaction were mapped. The VPg C-terminal region (38 amino acids) was important for the VPg–VPg interaction and the central 19 amino acids were needed for the HCPro–VPg interaction.

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