Structures of the mumps virus polymerase complex via cryo-electron microscopy

Tianhao Li, Mingdong Liu, Zhanxi Gu, Xin Su, Yunhui Liu, Jinzhong Lin, Yu Zhang and Qing-Tao Shen ()
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Tianhao Li: Southern University of Science and Technology
Mingdong Liu: Southern University of Science and Technology
Zhanxi Gu: University of Chinese Academy of Sciences
Xin Su: Southern University of Science and Technology
Yunhui Liu: Southern University of Science and Technology
Jinzhong Lin: Fudan University
Yu Zhang: Chinese Academy of Sciences
Qing-Tao Shen: Southern University of Science and Technology

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract The viral polymerase complex, comprising the large protein (L) and phosphoprotein (P), is crucial for both genome replication and transcription in non-segmented negative-strand RNA viruses (nsNSVs), while structures corresponding to these activities remain obscure. Here, we resolved two L–P complex conformations from the mumps virus (MuV), a typical member of nsNSVs, via cryogenic-electron microscopy. One conformation presents all five domains of L forming a continuous RNA tunnel to the methyltransferase domain (MTase), preferably as a transcription state. The other conformation has the appendage averaged out, which is inaccessible to MTase. In both conformations, parallel P tetramers are revealed around MuV L, which, together with structures of other nsNSVs, demonstrates the diverse origins of the L-binding X domain of P. Our study links varying structures of nsNSV polymerase complexes with genome replication and transcription and points to a sliding model for polymerase complexes to advance along the RNA templates.

Date: 2024
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DOI: 10.1038/s41467-024-48389-9

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