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TitleStructural basis for recognition and regulation of arenavirus polymerase L by Z protein.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 4134, Year 2021
Publish dateJul 5, 2021
AuthorsHuiling Kang / Jingyuan Cong / Chenlong Wang / Wenxin Ji / Yuhui Xin / Ying Qian / Xuemei Li / Yutao Chen / Zihe Rao /
PubMed AbstractJunin virus (JUNV) causes Argentine hemorrhagic fever, a debilitating human disease of high mortality rates and a great risk to public health worldwide. Studying the L protein that replicates and ...Junin virus (JUNV) causes Argentine hemorrhagic fever, a debilitating human disease of high mortality rates and a great risk to public health worldwide. Studying the L protein that replicates and transcribes the genome of JUNV, and its regulator Z protein should provide critical clues to identify therapeutic targets for disrupting the life cycle of JUNV. Here we report the 3.54 Å cryo-EM structure of the JUNV L protein complexed with regulator Z protein. JUNV L structure reveals a conserved architecture containing signature motifs found in other L proteins. Structural analysis shows that L protein is regulated by binding of Z protein at the RNA product exit site. Based on these findings, we propose a model for the role of Z protein as a switch to turn on/off the viral RNA synthesis via its interaction with L protein. Our work unveils the mechanism of JUNV transcription, replication and regulation, which provides a framework for the rational design of antivirals for combating viral infections.
External linksNat Commun / PubMed:34226547 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

31163

7eju

EMDB-31163, PDB-7eju:
Junin virus(JUNV) RNA polymerase L complexed with Z protein
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • junin mammarenavirus
KeywordsVIRAL PROTEIN / Junin virus / RNA polymerase / L protein / Z protein

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