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Structural basis for the unique molecular properties of broad-range phospholipase C from Listeria monocytogenes

Author

Listed:
  • Nejc Petrišič

    (National Institute of Chemistry
    University of Ljubljana)

  • Maksimiljan Adamek

    (National Institute of Chemistry)

  • Andreja Kežar

    (National Institute of Chemistry)

  • Samo B. Hočevar

    (National Institute of Chemistry)

  • Ema Žagar

    (National Institute of Chemistry)

  • Gregor Anderluh

    (National Institute of Chemistry)

  • Marjetka Podobnik

    (National Institute of Chemistry)

Abstract

Listeriosis is one of the most serious foodborne diseases caused by the intracellular bacterium Listeria monocytogenes. Its two major virulence factors, broad-range phospholipase C (LmPC-PLC) and the pore-forming toxin listeriolysin O (LLO), enable the bacterium to spread in the host by destroying cell membranes. Here, we determine the crystal structure of LmPC-PLC and complement it with the functional analysis of this enzyme. This reveals that LmPC-PLC has evolved several structural features to regulate its activity, including the invariant position of the N-terminal tryptophan (W1), the structurally plastic active site, Zn2+-dependent activity, and the tendency to form oligomers with impaired enzymatic activity. We demonstrate that the enzymatic activity of LmPC-PLC can be specifically inhibited by its propeptide added in trans. Furthermore, we show that the phospholipase activity of LmPC-PLC facilitates the pore-forming activity of LLO and affects the morphology of LLO oligomerization on lipid membranes, revealing the multifaceted synergy of the two virulence factors.

Suggested Citation

  • Nejc Petrišič & Maksimiljan Adamek & Andreja Kežar & Samo B. Hočevar & Ema Žagar & Gregor Anderluh & Marjetka Podobnik, 2023. "Structural basis for the unique molecular properties of broad-range phospholipase C from Listeria monocytogenes," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-42134-4
    DOI: 10.1038/s41467-023-42134-4
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    References listed on IDEAS

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    1. Kathryn Tunyasuvunakool & Jonas Adler & Zachary Wu & Tim Green & Michal Zielinski & Augustin Žídek & Alex Bridgland & Andrew Cowie & Clemens Meyer & Agata Laydon & Sameer Velankar & Gerard J. Kleywegt, 2021. "Highly accurate protein structure prediction for the human proteome," Nature, Nature, vol. 596(7873), pages 590-596, August.
    2. Liyabona Mpondo & Kingsley Ehi Ebomah & Anthony Ifeanyi Okoh, 2021. "Multidrug-Resistant Listeria Species Shows Abundance in Environmental Waters of a Key District Municipality in South Africa," IJERPH, MDPI, vol. 18(2), pages 1-12, January.
    3. John Jumper & Richard Evans & Alexander Pritzel & Tim Green & Michael Figurnov & Olaf Ronneberger & Kathryn Tunyasuvunakool & Russ Bates & Augustin Žídek & Anna Potapenko & Alex Bridgland & Clemens Me, 2021. "Highly accurate protein structure prediction with AlphaFold," Nature, Nature, vol. 596(7873), pages 583-589, August.
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