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Cryo-EM structure of the respiratory syncytial virus RNA polymerase

Author

Listed:
  • Dongdong Cao

    (Emory University School of Medicine)

  • Yunrong Gao

    (Emory University School of Medicine)

  • Claire Roesler

    (Emory University School of Medicine)

  • Samantha Rice

    (Emory University School of Medicine)

  • Paul D’Cunha

    (Emory University School of Medicine)

  • Lisa Zhuang

    (Emory University School of Medicine)

  • Julia Slack

    (Emory University School of Medicine)

  • Mason Domke

    (Emory University School of Medicine)

  • Anna Antonova

    (Emory University School of Medicine)

  • Sarah Romanelli

    (Emory University School of Medicine)

  • Shayon Keating

    (Emory University School of Medicine)

  • Gabriela Forero

    (Emory University School of Medicine)

  • Puneet Juneja

    (Emory University School of Medicine)

  • Bo Liang

    (Emory University School of Medicine)

Abstract

The respiratory syncytial virus (RSV) RNA polymerase, constituted of a 250 kDa large (L) protein and tetrameric phosphoprotein (P), catalyzes three distinct enzymatic activities — nucleotide polymerization, cap addition, and cap methylation. How RSV L and P coordinate these activities is poorly understood. Here, we present a 3.67 Å cryo-EM structure of the RSV polymerase (L:P) complex. The structure reveals that the RNA dependent RNA polymerase (RdRp) and capping (Cap) domains of L interact with the oligomerization domain (POD) and C-terminal domain (PCTD) of a tetramer of P. The density of the methyltransferase (MT) domain of L and the N-terminal domain of P (PNTD) is missing. Further analysis and comparison with other RNA polymerases at different stages suggest the structure we obtained is likely to be at an elongation-compatible stage. Together, these data provide enriched insights into the interrelationship, the inhibitors, and the evolutionary implications of the RSV polymerase.

Suggested Citation

  • Dongdong Cao & Yunrong Gao & Claire Roesler & Samantha Rice & Paul D’Cunha & Lisa Zhuang & Julia Slack & Mason Domke & Anna Antonova & Sarah Romanelli & Shayon Keating & Gabriela Forero & Puneet Junej, 2020. "Cryo-EM structure of the respiratory syncytial virus RNA polymerase," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-019-14246-3
    DOI: 10.1038/s41467-019-14246-3
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    Cited by:

    1. Tianhao Li & Mingdong Liu & Zhanxi Gu & Xin Su & Yunhui Liu & Jinzhong Lin & Yu Zhang & Qing-Tao Shen, 2024. "Structures of the mumps virus polymerase complex via cryo-electron microscopy," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Jin Xie & Mohamed Ouizougun-Oubari & Li Wang & Guanglei Zhai & Daitze Wu & Zhaohu Lin & Manfu Wang & Barbara Ludeke & Xiaodong Yan & Tobias Nilsson & Lu Gao & Xinyi Huang & Rachel Fearns & Shuai Chen, 2024. "Structural basis for dimerization of a paramyxovirus polymerase complex," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Jack D. Whitehead & Hortense Decool & Cédric Leyrat & Loic Carrique & Jenna Fix & Jean-François Eléouët & Marie Galloux & Max Renner, 2023. "Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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