Authors: Side Hu, Heesu Kim, Pan Yang, Zishuo Yu, Barbara Ludeke, Shawna Mobilia, Junhua Pan, Margaret Stratton, Yuemin Bian, Rachel Fearns, Jonathan Abraham
Year: 2025
Journal: Cell
DOI: 10.1016/j.cell.2024.12.021
Summary
The paper determines the cryoelectron microscopy (cryo-EM) structure of the Nipah virus polymerase complex and performs structural, biophysical, and functional analyses to understand features critical for RNA replication and transcription. The findings could aid in the development of antivirals.
Key Findings
- Cryo-EM structure of the NiV L-P complex determined
- Docking studies with an inhibitor clarify mechanisms of intrinsic NiV L resistance
- Palm insert, zinc fingers, and P4 extension are critical for NiV L activity
- Intrusion loop plays an essential role in RNA replication
Methodology
- Study Type: Structural analysis/Functional analysis
Topics
Virology, Pharmacology
Relevance
The paper's findings have implications for understanding Nipah virus replication and developing antivirals.
Source
View the entire paper: File:Main (2).pdf