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Discovery of fungal surface NADases predominantly present in pathogenic species

Author

Listed:
  • Øyvind Strømland

    (University of Bergen)

  • Juha P. Kallio

    (University of Bergen)

  • Annica Pschibul

    (Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute)

  • Renate H. Skoge

    (University of Bergen)

  • Hulda M. Harðardóttir

    (University of Bergen)

  • Lars J. Sverkeli

    (University of Bergen
    University of Bergen)

  • Thorsten Heinekamp

    (Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute)

  • Olaf Kniemeyer

    (Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute)

  • Marie Migaud

    (University of South Alabama)

  • Mikhail V. Makarov

    (University of South Alabama)

  • Toni I. Gossmann

    (Bielefeld University
    University of Sheffield)

  • Axel A. Brakhage

    (Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute
    Friedrich Schiller University Jena)

  • Mathias Ziegler

    (University of Bergen)

Abstract

Nicotinamide adenine dinucleotide (NAD) is a key molecule in cellular bioenergetics and signalling. Various bacterial pathogens release NADase enzymes into the host cell that deplete the host’s NAD+ pool, thereby causing rapid cell death. Here, we report the identification of NADases on the surface of fungi such as the pathogen Aspergillus fumigatus and the saprophyte Neurospora crassa. The enzymes harbour a tuberculosis necrotizing toxin (TNT) domain and are predominately present in pathogenic species. The 1.6 Å X-ray structure of the homodimeric A. fumigatus protein reveals unique properties including N-linked glycosylation and a Ca2+-binding site whose occupancy regulates activity. The structure in complex with a substrate analogue suggests a catalytic mechanism that is distinct from those of known NADases, ADP-ribosyl cyclases and transferases. We propose that fungal NADases may convey advantages during interaction with the host or competing microorganisms.

Suggested Citation

  • Øyvind Strømland & Juha P. Kallio & Annica Pschibul & Renate H. Skoge & Hulda M. Harðardóttir & Lars J. Sverkeli & Thorsten Heinekamp & Olaf Kniemeyer & Marie Migaud & Mikhail V. Makarov & Toni I. Gos, 2021. "Discovery of fungal surface NADases predominantly present in pathogenic species," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21307-z
    DOI: 10.1038/s41467-021-21307-z
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    Cited by:

    1. Martin Hagan & Genady Pankov & Ramses Gallegos-Monterrosa & David J. Williams & Christopher Earl & Grant Buchanan & William N. Hunter & Sarah J. Coulthurst, 2023. "Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Xiangkai Zhen & Xiaolong Xu & Le Ye & Song Xie & Zhijie Huang & Sheng Yang & Yanhui Wang & Jinyu Li & Feng Long & Songying Ouyang, 2024. "Structural basis of antiphage immunity generated by a prokaryotic Argonaute-associated SPARSA system," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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