TitleStability of Begomoviral pathogenicity determinant βC1 is modulated by mutually antagonistic SUMOylation and SIM interactions.
Publication TypeJournal Article
Year of Publication2020
AuthorsNair A, Chatterjee KSankar, Jha V, Das R, Shivaprasad PV
JournalBMC Biol
Date Published2020 Aug 31

BACKGROUND: To successfully invade new hosts, plant viruses must break host resistance and be competent to move within and between plant cells. As a means, viral proteins known as pathogenicity determinants have evolved to coordinate a network of protein interactions. The βC1 protein encoded by specific geminiviral satellites acts as a key pathogenicity determinant for this disease-causing family of plant viruses. Post-translational modifications (PTMs) such as ubiquitination and phosphorylation of the βC1 protein have been shown to occur in diverse viruses. However, the relevance of these and other layers of PTMs in host-geminiviral interactions has not been fully understood.

RESULTS: Here we identified the significance of a novel layer of PTMs in the βC1 protein of Synedrella yellow vein clearing virus (SyYVCV), a newly identified member of the Begomovirus genus of Geminiviruses. This protein has conserved SUMOylation and SUMO-interacting motifs (SIMs), and we observed SUMOylation of SyYVCV βC1 in host plants as a defensive strategy against ubiquitin-mediated degradation. Counteracting this, SIMs encoded in βC1 mediate the degradation of βC1; however, both these PTMs are essential for the function of βC1 protein since SIM and SUMOylation motif mutants failed to promote pathogenicity and viral replication in vivo. SUMOylation in different motifs of βC1 led to functionally distinct outcomes, regulating the stability and function of the βC1 protein, as well as increased global SUMOylation of host proteins.

CONCLUSION: Our results indicate the presence of a novel mechanism mediating a fine balance between defence and counter-defence in which a SIM site is competitively sought for degradation and, as a counter-defence, βC1 undergoes SUMOylation to escape from its degradation.

Alternate JournalBMC Biol.
PubMed ID32867776
Grant ListBT/PR12394/AGIII/103/891/2014 / / Department of Biotechnology , Ministry of Science and Technology /
BT/IN/Swiss/47/JGK/2018-19 / / Department of Biotechnology , Ministry of Science and Technology /
BT/PR25767/GET/119/151/ 2017 / / Department of Biotechnology , Ministry of Science and Technology /
BT/HRD/23/02/2006 / / Science and Engineering Research Board /
Email to communications office: Email to communications office