Poster Presentation International Plant Molecular Biology Conference 2024

Characterization of protein-protein interactions involving the movement protein VP37 of broad bean wilt virus 2 (#72)

Sora Kim 1 , Myung-Hwi Kim 1 , Seok-Yeong Jang 1 , Sun-Jung Kwon 2 , Jang-Kyun Seo 1 2
  1. Department of International Agricultural Technology, Seoul National University, Pyeongchang, Gangwon, Republic of Korea
  2. Institutes of Green Bio Science and Technology, Seoul National University, Pyeongchang, Gangwon, Republic of Korea

Broad bean wilt virus 2 (BBWV2) is one of the prevalent viral pathogens in pepper. To date, there have been no reports of pepper cultivars resistant to BBWV2, necessitating the exploration of genetic resources for breeding BBWV2-resistant cultivars. The strategic approaches to acquiring such genetic resources involve elucidating the protein-protein interactions of viral proteins. Because viruses have a limited capacity for encoding own proteins due to their small genomes, they rely on the interactions among viral proteins and with host proteins for successful infection. In this regard, mutations that disrupt these interactions in either viral or host proteins could inhibit virus infection, thereby serving as genetic resources to confer resistance against viruses. In this study, we performed protein interaction screening assays, including yeast two-hybrid (Y2H) and co-immunoprecipitation (Co-IP), to identify viral and host proteins interacting with the BBWV2 proteins. Y2H revealed that VP37, the movement protein of BBWV2, interacted strongly with the viral protease (Pro). We also identified the crucial amino acid residues of VP37 associated in the interaction with Pro. In addition, Co-IP identified the host actin protein as an interacting partner of VP37. Inhibition of actin microfilament polymerization resulted in the suppression of systemic spread of BBWV2, suggesting that BBWV2 utilize host actin microfilaments for viral intracellular movement. Our findings provide a deeper insight into the protein interaction network of BBWV2 and suggest novel target points that could enhance resistance against BBWV2.