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Glycan-dependent cell adhesion mechanism of Tc toxins

Author

Listed:
  • Daniel Roderer

    (Max Planck Institute of Molecular Physiology)

  • Felix Bröcker

    (Max Planck Institute of Colloids and Interfaces
    Vaxxilon Deutschland GmbH)

  • Oleg Sitsel

    (Max Planck Institute of Molecular Physiology)

  • Paulina Kaplonek

    (Max Planck Institute of Colloids and Interfaces
    Ragon Institute of MGH, MIT and Harvard)

  • Franziska Leidreiter

    (Max Planck Institute of Molecular Physiology
    Max Planck Institute for Medical Research)

  • Peter H. Seeberger

    (Max Planck Institute of Colloids and Interfaces)

  • Stefan Raunser

    (Max Planck Institute of Molecular Physiology)

Abstract

Toxin complex (Tc) toxins are virulence factors of pathogenic bacteria. Tcs are composed of three subunits: TcA, TcB and TcC. TcA facilitates receptor–toxin interaction and membrane permeation, TcB and TcC form a toxin-encapsulating cocoon. While the mechanisms of holotoxin assembly and pore formation have been described, little is known about receptor binding of TcAs. Here, we identify heparins/heparan sulfates and Lewis antigens as receptors for different TcAs from insect and human pathogens. Glycan array screening reveals that all tested TcAs bind negatively charged heparins. Cryo-EM structures of Morganella morganii TcdA4 and Xenorhabdus nematophila XptA1 reveal that heparins/heparan sulfates unexpectedly bind to different regions of the shell domain, including receptor-binding domains. In addition, Photorhabdus luminescens TcdA1 binds to Lewis antigens with micromolar affinity. Here, the glycan interacts with the receptor-binding domain D of the toxin. Our results suggest a glycan dependent association mechanism of Tc toxins on the host cell surface.

Suggested Citation

  • Daniel Roderer & Felix Bröcker & Oleg Sitsel & Paulina Kaplonek & Franziska Leidreiter & Peter H. Seeberger & Stefan Raunser, 2020. "Glycan-dependent cell adhesion mechanism of Tc toxins," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16536-7
    DOI: 10.1038/s41467-020-16536-7
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    Cited by:

    1. Alexander Belyy & Florian Lindemann & Daniel Roderer & Johanna Funk & Benjamin Bardiaux & Jonas Protze & Peter Bieling & Hartmut Oschkinat & Stefan Raunser, 2022. "Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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