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TitleStructural basis for dimerization of a paramyxovirus polymerase complex.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3163, Year 2024
Publish dateApr 11, 2024
AuthorsJin Xie / Mohamed Ouizougun-Oubari / Li Wang / Guanglei Zhai / Daitze Wu / Zhaohu Lin / Manfu Wang / Barbara Ludeke / Xiaodong Yan / Tobias Nilsson / Lu Gao / Xinyi Huang / Rachel Fearns / Shuai Chen /
PubMed AbstractThe transcription and replication processes of non-segmented, negative-strand RNA viruses (nsNSVs) are catalyzed by a multi-functional polymerase complex composed of the large protein (L) and a ...The transcription and replication processes of non-segmented, negative-strand RNA viruses (nsNSVs) are catalyzed by a multi-functional polymerase complex composed of the large protein (L) and a cofactor protein, such as phosphoprotein (P). Previous studies have shown that the nsNSV polymerase can adopt a dimeric form, however, the structure of the dimer and its function are poorly understood. Here we determine a 2.7 Å cryo-EM structure of human parainfluenza virus type 3 (hPIV3) L-P complex with the connector domain (CD') of a second L built, while reconstruction of the rest of the second L-P obtains a low-resolution map of the ring-like L core region. This study reveals detailed atomic features of nsNSV polymerase active site and distinct conformation of hPIV3 L with a unique β-strand latch. Furthermore, we report the structural basis of L-L dimerization, with CD' located at the putative template entry of the adjoining L. Disruption of the L-L interface causes a defect in RNA replication that can be overcome by complementation, demonstrating that L dimerization is necessary for hPIV3 genome replication. These findings provide further insight into how nsNSV polymerases perform their functions, and suggest a new avenue for rational drug design.
External linksNat Commun / PubMed:38605025 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.3 Å
Structure data

37130

8kdb

EMDB-37130, PDB-8kdb:
Cryo-EM structure of the human parainfluenza virus hPIV3 L-P polymerase in dimeric form
Method: EM (single particle) / Resolution: 2.7 Å

37131

8kdc

EMDB-37131, PDB-8kdc:
Cryo-EM structure of the human parainfluenza virus hPIV3 L-P polymerase in monomeric form
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • human respirovirus 3
KeywordsVIRAL PROTEIN / dimeric polymerase / parainfluenza virus / L-P polymerase / cryo-EM structure / non-segmented negative-strand RNA virus / L-L dimerization / RNA replication / RdRp active site

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