Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses
Peer-Reviewed Publication
Updates every hour. Last Updated: 21-Jul-2025 10:11 ET (21-Jul-2025 14:11 GMT/UTC)
This study reports two cryo-EM structures of the Nipah virus (NiV) polymerase L-P complex in its full-length and truncated forms. These structures elucidate the RNA-dependent RNA polymerase (RdRp) and polyribonucleotidyl transferase (PRNTase) domains of the L protein, as well as the tetrameric P protein bundle bound to the L-RdRp. This work establishes a foundational framework for understanding the NiV polymerase mechanism and provides critical insights for the rational design of antiviral therapeutics targeting the polymerase complex
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