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

Huiling Kang, Jingyuan Cong, Chenlong Wang, Wenxin Ji, Yuhui Xin, Ying Qian, Xuemei Li (), Yutao Chen () and Zihe Rao
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Huiling Kang: Chinese Academy of Sciences
Jingyuan Cong: Chinese Academy of Sciences
Chenlong Wang: Chinese Academy of Sciences
Wenxin Ji: Chinese Academy of Sciences
Yuhui Xin: 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

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-021-24458-1

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