tetano
Editor, Senior Moderator
Nat Commun
. 2025 Nov 4;16(1):9741.
doi: 10.1038/s41467-025-64741-z. Coupling of polymerase-nucleoprotein-RNA in an influenza virus mini ribonucleoprotein complex
Huiling Kang[SUP] #[/SUP][SUP] 1 2 3 4 [/SUP], Yunxiang Yang[SUP] #[/SUP][SUP] 2 [/SUP], Yixiao Liu[SUP] #[/SUP][SUP] 2 [/SUP], Mingyu Li[SUP] #[/SUP][SUP] 2 [/SUP], Lejin Zhang[SUP] #[/SUP][SUP] 5 [/SUP], Yuqi Lin[SUP] 5 [/SUP], Leander Witte[SUP] 6 [/SUP], Kuang-Yu Chen[SUP] 6 [/SUP], Wenya Song[SUP] 7 [/SUP], Zhili Xu[SUP] 5 [/SUP], Xiaojing He[SUP] 8 [/SUP], Luke W Guddat[SUP] 9 [/SUP], Yu Guo[SUP] 10 [/SUP], Liming Yan[SUP] 2 [/SUP], Yan Gao[SUP] 1 [/SUP], Ervin Fodor[SUP] 11 [/SUP], Zihe Rao[SUP] 12 13 14 15 16 17 [/SUP], Zhiyong Lou[SUP] 18 19 [/SUP]
Affiliations
Influenza virus ribonucleoprotein complexes (RNPs), composed of the polymerase complex (FluPol), nucleoprotein (NP), and RNA, are essential for replication and transcription. We report atomic-resolution cryo-EM structures of mini-vRNPs in two states: FluPol located inside (State-In) or at the outer rim (State-Out) of the NP-RNA ring. In both states, the 5' and 3' termini of vRNA are bound to FluPol as previously reported. One NP (NP-0) contacts PA/PB1 of FluPol and binds the distal double-stranded vRNA promoter, with its D72-K90 loop inserting into the RNA fork; separated strands occupy NP-0 RNA-binding grooves. Grooves from other NPs form a continuous RNA-protective path, consistent with negative-strand RNA virus mechanisms. In State-In, interfaces for FluPol dimerization or Pol II interaction are blocked, but fully exposed in State-Out. These structures reveal detailed FluPol-NP-RNA coupling and suggest a conformational shift in RNPs during the viral life cycle.
. 2025 Nov 4;16(1):9741.
doi: 10.1038/s41467-025-64741-z. Coupling of polymerase-nucleoprotein-RNA in an influenza virus mini ribonucleoprotein complex
Huiling Kang[SUP] #[/SUP][SUP] 1 2 3 4 [/SUP], Yunxiang Yang[SUP] #[/SUP][SUP] 2 [/SUP], Yixiao Liu[SUP] #[/SUP][SUP] 2 [/SUP], Mingyu Li[SUP] #[/SUP][SUP] 2 [/SUP], Lejin Zhang[SUP] #[/SUP][SUP] 5 [/SUP], Yuqi Lin[SUP] 5 [/SUP], Leander Witte[SUP] 6 [/SUP], Kuang-Yu Chen[SUP] 6 [/SUP], Wenya Song[SUP] 7 [/SUP], Zhili Xu[SUP] 5 [/SUP], Xiaojing He[SUP] 8 [/SUP], Luke W Guddat[SUP] 9 [/SUP], Yu Guo[SUP] 10 [/SUP], Liming Yan[SUP] 2 [/SUP], Yan Gao[SUP] 1 [/SUP], Ervin Fodor[SUP] 11 [/SUP], Zihe Rao[SUP] 12 13 14 15 16 17 [/SUP], Zhiyong Lou[SUP] 18 19 [/SUP]
Affiliations
- PMID: 41188214
- DOI: 10.1038/s41467-025-64741-z
Influenza virus ribonucleoprotein complexes (RNPs), composed of the polymerase complex (FluPol), nucleoprotein (NP), and RNA, are essential for replication and transcription. We report atomic-resolution cryo-EM structures of mini-vRNPs in two states: FluPol located inside (State-In) or at the outer rim (State-Out) of the NP-RNA ring. In both states, the 5' and 3' termini of vRNA are bound to FluPol as previously reported. One NP (NP-0) contacts PA/PB1 of FluPol and binds the distal double-stranded vRNA promoter, with its D72-K90 loop inserting into the RNA fork; separated strands occupy NP-0 RNA-binding grooves. Grooves from other NPs form a continuous RNA-protective path, consistent with negative-strand RNA virus mechanisms. In State-In, interfaces for FluPol dimerization or Pol II interaction are blocked, but fully exposed in State-Out. These structures reveal detailed FluPol-NP-RNA coupling and suggest a conformational shift in RNPs during the viral life cycle.