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TitleStructure of the Respiratory Syncytial Virus Polymerase Complex.
Journal, issue, pagesCell, Vol. 179, Issue 1, Page 193-204.e14, Year 2019
Publish dateSep 19, 2019
AuthorsMorgan S A Gilman / Cheng Liu / Amy Fung / Ishani Behera / Paul Jordan / Peter Rigaux / Nina Ysebaert / Sergey Tcherniuk / Julien Sourimant / Jean-François Eléouët / Priscila Sutto-Ortiz / Etienne Decroly / Dirk Roymans / Zhinan Jin / Jason S McLellan /
PubMed AbstractNumerous interventions are in clinical development for respiratory syncytial virus (RSV) infection, including small molecules that target viral transcription and replication. These processes are ...Numerous interventions are in clinical development for respiratory syncytial virus (RSV) infection, including small molecules that target viral transcription and replication. These processes are catalyzed by a complex comprising the RNA-dependent RNA polymerase (L) and the tetrameric phosphoprotein (P). RSV P recruits multiple proteins to the polymerase complex and, with the exception of its oligomerization domain, is thought to be intrinsically disordered. Despite their critical roles in RSV transcription and replication, structures of L and P have remained elusive. Here, we describe the 3.2-Å cryo-EM structure of RSV L bound to tetrameric P. The structure reveals a striking tentacular arrangement of P, with each of the four monomers adopting a distinct conformation. The structure also rationalizes inhibitor escape mutants and mutations observed in live-attenuated vaccine candidates. These results provide a framework for determining the molecular underpinnings of RSV replication and transcription and should facilitate the design of effective RSV inhibitors.
External linksCell / PubMed:31495574 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

20536

6pzk

EMDB-20536, PDB-6pzk:
Cryo-EM Structure of the Respiratory Syncytial Virus Polymerase (L) Protein Bound by the Tetrameric Phosphoprotein (P)
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • human respiratory syncytial virus a2
KeywordsVIRAL PROTEIN / RNA-binding protein / RSV / RdRp / RNA-dependent RNA polymerase / PRNTase / polyribonucleotidyl transferase / RNA capping / viral replication

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