Intrinsic disorder in flaviviral capsid proteins and its role in pathogenesis
No Thumbnail Available
Date
2024-05
Journal Title
Journal ISSN
Volume Title
Publisher
The Indian Academy of Sciences
Abstract
A high level of disorder in many viral proteins is a direct consequence of their small genomes, which makes interaction with multiple binding partners a necessity for infection and pathogenicity. A segment of the flaviviral capsid protein (C), also known as the molecular recognition feature (MoRF), undergoes a disorder-to-order transition upon binding to several protein partners. To understand their role in pathogenesis, MoRFs were identified and their occurrence across different flaviviral capsids were studied. Despite lack of sequence similarities, docking studies of Cs with the host proteins indicate conserved interactions involving MoRFs across members of phylogenetic subclades. Additionally, it was observed from the protein–protein networks that some MoRFs preferentially bind proteins that are involved in specialized functions such as ribosome biogenesis. The findings point to the importance of MoRFs in the flaviviral life cycle, with important consequences for disease progression and suppression of the host immune system. Potentially, they might have impacted the way flaviviruses evolved to infect varied hosts using multiple vectors.
Description
Keywords
Interaction, intrinsically disordered proteins, molecular recognition feature, structure, virus
Citation
SUNDAR ANIRUDH, UMASHANKAR PAVITHRA, SANKAR PRIYANKA, RAMASAMY KAVITHA, VENKATARAMAN SANGITA. Intrinsic disorder in flaviviral capsid proteins and its role in pathogenesis. Journal of Biosciences. 2024 May; 49: 1-12