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Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states

Nature volume 367, pages 292–295 (1994)Cite this article

Abstract

AEROLYSIN is chiefly responsible for the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections1. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that destroys sensitive cells by breaking their permeability barriers2. Here we describe the structure of proaerolysin determined by X-ray crystallography at 2.8 Å resolution. The protoxin (Mr 52,000) adopts a novel protein fold. Images of an aerolysin oligomer derived from electron microscopy have assisted in constructing a model of the membrane channel and have led to the proposal of a scheme to account for insertion of the protein into lipid bilayers to form ion channels.

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Author notes

  1. Alec D. Tucker

    Present address: ZENECA Pharmaceuticals, Alderley Park, Macclesfield, Cheshire, SK104TG, UK

Authors and Affiliations

  1. St Vincent's Institute of Medical Research, 41 Victoria Parade, Fitzroy, Victoria, 3065, Australia

    Michael W. Parker

  2. Department of Biochemistry and Microbiology, University of Victoria, British Columbia, V8W 2Y2, Canada

    J. Thomas Buckley

  3. European Molecular Biology Laboratory, Meyerhofstrasse 1, D-6900, Heidelberg, Germany

    Johan P. M. Postma, Alec D. Tucker, Kevin Leonard, Franc Pattus & Demetrius Tsernoglou

Authors
  1. Michael W. Parker
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  2. J. Thomas Buckley
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  3. Johan P. M. Postma
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  4. Alec D. Tucker
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  5. Kevin Leonard
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  6. Franc Pattus
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  7. Demetrius Tsernoglou
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Parker, M., Buckley, J., Postma, J. et al. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367, 292–295 (1994). https://doi.org/10.1038/367292a0

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