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TitleOrchestrated and dynamic nucleotide addition cycle during respiratory syncytial virus early-stage elongation.
Journal, issue, pagesNat Commun, Year 2026
Publish dateApr 29, 2026
AuthorsDongdong Cao / Zhenhang Chen / Yunrong Gao / Claire Roesler / Inesh Gooneratne / Cristopher Mera / Lisa Zhuang / Julia Slack / Elijah Nudell-Cook / Jenny Vy / Jasmine Berry / Maurice Royal / Masthan Shaik / Ryan Youngs / Bo Liang /
PubMed AbstractThe respiratory syncytial virus (RSV) polymerase (L:P complex) is responsible for viral RNA transcription and replication, where nucleotide addition cycles (NACs) are executed repeatedly during ...The respiratory syncytial virus (RSV) polymerase (L:P complex) is responsible for viral RNA transcription and replication, where nucleotide addition cycles (NACs) are executed repeatedly during elongation in both processes. Using cryo-EM, we capture snapshots of RSV polymerase in action during early-stage elongation and in four distinct NAC states: NTP-bound, pre-reaction, pre-translocation, and post-translocation. Strikingly, we observe all five domains of RSV L in NTP-bound and post-translocation states. In contrast, only two domains are visible in pre-reaction and pre-translocation states, similar to previously reported apo or promoter-bound structures. Importantly, these snapshots reveal the synergistic and dynamic interaction networks among key residues and motifs of RSV polymerase, RNA template, product, incoming nucleotide, and metal ions across NAC states. Our findings provide the first comprehensive insights into orchestrated macro-domain rearrangements and micro-motif changes of RSV polymerase during NAC catalysis, facilitating antiviral therapeutics targeting RSV and related nonsegmented negative-sense RNA viruses, including rabies, Nipah, and Ebola.
External linksNat Commun / PubMed:42049741
MethodsEM (single particle)
Resolution2.75 - 3.54 Å
Structure data

71611

9pfr

EMDB-71611, PDB-9pfr:
Cryo-EM structure of the respiratory syncytial virus polymerase (L:P) in NTP-bound elongation state
Method: EM (single particle) / Resolution: 3.08 Å

71612

9pfs

EMDB-71612, PDB-9pfs:
Cryo-EM structure of the respiratory syncytial virus polymerase (L:P) in pre-reaction elongation state
Method: EM (single particle) / Resolution: 2.75 Å

71613

9pft

EMDB-71613, PDB-9pft:
Cryo-EM structure of the respiratory syncytial virus polymerase (L:P) in pre-translocation elongation state
Method: EM (single particle) / Resolution: 3.07 Å

71614

9pfu

EMDB-71614, PDB-9pfu:
Cryo-EM structure of the respiratory syncytial virus polymerase (L:P) in post-translocation elongation state
Method: EM (single particle) / Resolution: 3.54 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZAN:
5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]adenosine

Source
  • respiratory syncytial virus a2
  • respiratory syncytial virus
KeywordsVIRAL PROTEIN / TRANSFERASE/RNA / Respiratory syncytial virus / RNA-dependent RNA polymerase / nucleotide addition cycle / VIRAL PROTEIN-RNA complex / TRANSFERASE-RNA complex

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