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Structural basis for recognition and regulation of arenavirus polymerase L by Z protein

Author

Listed:
  • Huiling Kang

    (Chinese Academy of Sciences
    Sichuan University)

  • Jingyuan Cong

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Chenlong Wang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Wenxin Ji

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Yuhui Xin

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Ying Qian

    (Chinese Academy of Sciences)

  • Xuemei Li

    (Chinese Academy of Sciences)

  • Yutao Chen

    (Chinese Academy of Sciences)

  • Zihe Rao

    (Chinese Academy of Sciences
    Tsinghua University)

Abstract

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.

Suggested Citation

  • Huiling Kang & Jingyuan Cong & Chenlong Wang & Wenxin Ji & Yuhui Xin & Ying Qian & Xuemei Li & Yutao Chen & Zihe Rao, 2021. "Structural basis for recognition and regulation of arenavirus polymerase L by Z protein," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24458-1
    DOI: 10.1038/s41467-021-24458-1
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    Cited by:

    1. Tomas Kouba & Dominik Vogel & Sigurdur R. Thorkelsson & Emmanuelle R. J. Quemin & Harry M. Williams & Morlin Milewski & Carola Busch & Stephan Günther & Kay Grünewald & Maria Rosenthal & Stephen Cusac, 2021. "Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity," Nature Communications, Nature, vol. 12(1), pages 1-18, December.
    2. Jun Ma & Shuangyue Zhang & Xinzheng Zhang, 2021. "Structure of Machupo virus polymerase in complex with matrix protein Z," Nature Communications, Nature, vol. 12(1), pages 1-8, December.

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