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Staphylococcal alpha-toxin

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Microbial Protein Toxins

Part of the book series: Topics in Current Genetics ((TCG,volume 11))

Abstract

Staphylococcal alpha-toxin, archetype of an oligomerizing pore-forming toxin, is produced and secreted as a water-soluble 34 kD monomer. High affinity binding possibly occurs to clustered phosphocholine head groups in cholesterol/sphingomyelin-rich membrane microdomains. Toxin heptamers can rapidly assemble at such sites, and oligomerization triggers conformational changes leading to insertion of an amphipathic hairpin b-barrel sequence into the lipid bilayer, so that a protein-lined pore of approximately 1 nm diameter is formed. Many cellular reactions are triggered by the uncontrolled transmembrane flux of ions, and these can account for short- and long-range effects of the toxin. Moreover, nucleated cells can repair a limited number of membrane lesions, and transcriptional responses are then triggered that further contribute to long-term effects of the toxin. The biological relevance of the toxin is well established, and novel prophylactic and therapeutic strategies targeting this major virulence factor of S. aureus are currently being developed.

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Authors and Affiliations

  1. Institute of Medical Microbiology and Hygiene, Johannes Gutenberg-University Mainz, Hochhaus am Augustusplatz, D-55101 Mainz, Germany

    Sucharit Bhakdi, Iwan Walev, Matthias Husmann & Angela Valeva

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  1. Sucharit Bhakdi
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  2. Iwan Walev
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  3. Matthias Husmann
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  4. Angela Valeva
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Correspondence to Sucharit Bhakdi .

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Manfred J. Schmitt Raffael Schaffrath

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Bhakdi, S., Walev, I., Husmann, M., Valeva, A. Staphylococcal alpha-toxin. In: Schmitt, M.J., Schaffrath, R. (eds) Microbial Protein Toxins. Topics in Current Genetics, vol 11. Springer, Berlin, Heidelberg. https://doi.org/10.1007/b100513

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