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Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex

Author

Listed:
  • Hyunmin Kim

    (Korea Advanced Institute of Science and Technology)

  • Tomoko Kubori

    (Gifu University)

  • Kohei Yamazaki

    (Gifu University
    Kitasato University)

  • Mi-Jeong Kwak

    (Korea Advanced Institute of Science and Technology
    CKD Research Institute)

  • Suk-Youl Park

    (POSTECH)

  • Hiroki Nagai

    (Gifu University)

  • Joseph P. Vogel

    (Washington University School of Medicine)

  • Byung-Ha Oh

    (Korea Advanced Institute of Science and Technology)

Abstract

The Legionella pneumophila Dot/Icm type IVB secretion system (T4BSS) is extremely versatile, translocating ~300 effector proteins into host cells. This specialized secretion system employs the Dot/Icm type IVB coupling protein (T4CP) complex, which includes IcmS, IcmW and LvgA, that are known to selectively assist the export of a subclass of effectors. Herein, the crystal structure of a four-subunit T4CP subcomplex bound to the effector protein VpdB reveals an interaction between LvgA and a linear motif in the C-terminus of VpdB. The same binding interface of LvgA also interacts with the C-terminal region of three additional effectors, SidH, SetA and PieA. Mutational analyses identified a FxxxLxxxK binding motif that is shared by VpdB and SidH, but not by SetA and PieA, showing that LvgA recognizes more than one type of binding motif. Together, this work provides a structural basis for how the Dot/Icm T4CP complex recognizes effectors, and highlights the multiple substrate-binding specificities of its adaptor subunit.

Suggested Citation

  • Hyunmin Kim & Tomoko Kubori & Kohei Yamazaki & Mi-Jeong Kwak & Suk-Youl Park & Hiroki Nagai & Joseph P. Vogel & Byung-Ha Oh, 2020. "Structural basis for effector protein recognition by the Dot/Icm Type IVB coupling protein complex," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16397-0
    DOI: 10.1038/s41467-020-16397-0
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    Cited by:

    1. Rahul Sharma & Michael Adams & Simonne Griffith-Jones & Tobias Sahr & Laura Gomez-Valero & Felix Weis & Michael Hons & Sarah Gharbi & Rayene Berkane & Alexandra Stolz & Carmen Buchrieser & Sagar Bhoga, 2023. "Structural basis for the toxicity of Legionella pneumophila effector SidH," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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