RT Journal Article
SR Electronic
T1 Knockdown of a novel ATPase domain of capsid protein inhibits genome packaging in potato leaf roll virus
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.05.24.445413
DO 10.1101/2021.05.24.445413
A1 Jitesh Kumar
A1 Ravi Ranjan Kumar
A1 Dilip Kumar Das
A1 Auroshikha Mohanty
A1 Kumari Rajani
A1 Namaste Kumari
A1 Vinod Kumar
A1 Sunil Kumar
A1 Tushar Ranjan
YR 2021
UL http://biorxiv.org/content/early/2021/05/24/2021.05.24.445413.abstract
AB Potato leaf roll virus (PLRV) uses powerful molecular machines to package its genome into a viral capsid employing ATP as fuel. Although, recent bioinformatics and structural studies have revealed detailed mechanism of DNA packaging, little is known about the mechanochemistry of genome packaging in small plant viruses such as PLRV. We have identified a novel P-loop-containing ATPase domain with two Walker A-like motifs, two arginine fingers, and two sensor motifs distributed throughout the polypeptide chain of PLRV capsid protein (CP). The composition and arrangement of the ATP binding and hydrolysis domain of PLRV CP is unique and rarely reported. The discovery of the system sheds new light on the mechanism of viral genome packaging, regulation of viral assembly process, and evolution of plant viruses. Here, we used the RNAi approach to suppress CP gene expression, which in turn prevented PLRV genome packaging and assembly in Solanum tuberosum cv. Khufri Ashoka. Potato plants agroinfiltrated with siRNA constructs against the ATPase domain of CP exhibited no rolling symptoms upon PLRV infection, indicating that the silencing of CP gene expression is an efficient method for generating PLRV-resistant potato plants. Moreover, our findings provide a robust approach to generate PLRV-resistant potato plants, which can be further extended to other species. Finally, we propose a new mechanism of genome packaging and assembly in plant viruses.Competing Interest StatementThe authors have declared no competing interest.