Structure of the Newcastle Disease Virus L protein in complex with tetrameric phosphoprotein

Jingyuan Cong, Xiaoying Feng, Huiling Kang, Wangjun Fu, Lei Wang, Chenlong Wang, Xuemei Li (), Yutao Chen () and Zihe Rao
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Jingyuan Cong: Institute of Biophysics, Chinese Academy of Sciences
Xiaoying Feng: Institute of Biophysics, Chinese Academy of Sciences
Huiling Kang: Tsinghua University
Wangjun Fu: Institute of Biophysics, Chinese Academy of Sciences
Lei Wang: Institute of Biophysics, Chinese Academy of Sciences
Chenlong Wang: Tsinghua University
Xuemei Li: Institute of Biophysics, Chinese Academy of Sciences
Yutao Chen: Institute of Biophysics, Chinese Academy of Sciences
Zihe Rao: Institute of Biophysics, Chinese Academy of Sciences

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract Newcastle disease virus (NDV) belongs to Paramyxoviridae, which contains lethal human and animal pathogens. NDV RNA genome is replicated and transcribed by a multifunctional 250 kDa RNA-dependent RNA polymerase (L protein). To date, high-resolution structure of NDV L protein complexed with P protein remains to be elucidated, limiting our understanding of the molecular mechanisms of Paramyxoviridae replication/transcription. Here, we used cryo-EM and enzymatic assays to investigate the structure-function relationship of L-P complex. We found that C-terminal of CD-MTase-CTD module of the atomic-resolution L-P complex conformationally rearranges, and the priming/intrusion loops are likely in RNA elongation conformations different from previous structures. The P protein adopts a unique tetrameric organization and interacts with L protein. Our findings indicate that NDV L-P complex represents elongation state distinct from previous structures. Our work greatly advances the understanding of Paramyxoviridae RNA synthesis, revealing how initiation/elongation alternates, providing clues for identifying therapeutic targets against Paramyxoviridae.

Date: 2023
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DOI: 10.1038/s41467-023-37012-y

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