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Pseudomonas aeruginosa Exoenzyme S

  • Chapter
ADP-Ribosylating Toxins

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 175))

Abstract

Pseudomonas aeruginosa is an opportunistic pathogen that secretes a number of potential virulence factors. Two of these, exotoxin A and exoenzyme S, catalyze the transfer of the ADP-ribose moiety of NAD to proteins in eukaryotic cells. Exotoxin A catalyzes the ADP-ribosylation of elongation factor 2 (EF-2), leading to disruption of protein synthesis. It has been well characterized and is reviewed elsewhere in this volume. Exoenzyme S has been less thoroughly studied, but several lines of evidence suggest that it might play a role in pathogenesis. In preliminary experiments exoenzyme S appeared to be unselective in choice of substrate proteins, but recent work has shown that it preferentially ADP-ribosylates several of the low-molecular weight GTP-binding proteins. Furthermore, like cholera toxin, exoenzyme S requires a eukaryotic protein for enzymic activity.

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Author notes

  1. J. Coburn

    Present address: Division of Rheumatology and Immunology, New England Medical Center, Box 406, 750 Washington St., 02111, Boston, MA, USA

Authors and Affiliations

  1. Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Avenue, 02111, Boston, MA, USA

    J. Coburn

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  1. J. Coburn
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Editors and Affiliations

  1. Institut für Pharmakologie und Toxikologie, Universität des Saarlands, 6650, Homburg/saar, Germany

    Klaus Aktories

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© 1992 Springer-Verlag Berlin · Heidelberg

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Coburn, J. (1992). Pseudomonas aeruginosa Exoenzyme S. In: Aktories, K. (eds) ADP-Ribosylating Toxins. Current Topics in Microbiology and Immunology, vol 175. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76966-5_7

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  • DOI: https://doi.org/10.1007/978-3-642-76966-5_7

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-76968-9

  • Online ISBN: 978-3-642-76966-5

  • eBook Packages: Springer Book Archive

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