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Structure and dynamics of the Nipah virus RNA-dependent RNA polymerase.

Jul 2026 · TIBS -Trends in Biochemical Sciences. Regular ed · Vol 51, pp. 924-936 · 0 citations · 46 references
Medicine

TL;DR

How snapshots of the NiV RdRp complex in precatalytic, early-elongation, and inhibitor-bound states shed light on the molecular mechanisms of RNA synthesis and inhibition in NiV is reviewed and how these insights expand the understanding of nsNSV RdRps in general is explored.

Abstract

Nipah virus (NiV) is a highly pathogenic, nonsegmented, negative-sense RNA virus (nsNSV) from the Mononegavirales order that causes frequent outbreaks, with no approved treatment available. Replication and transcription of its genome are carried out by a viral RNA-dependent RNA polymerase (RdRp) complex composed of the large catalytic protein (L) and the tetrameric phosphoprotein (P). Recently, structural insights into the NiV RdRp complex have emerged at an unprecedented pace. In particular, snapshots of the complex in precatalytic, early-elongation, and inhibitor-bound states have been reported. In this article, we review how these data shed light on the molecular mechanisms of RNA synthesis and inhibition in NiV and explore how these insights expand our understanding of nsNSV RdRps in general.

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