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| PROSITE documentation PDOC00436 |
Thiol-activated cytolysins signature
Thiol-activated cytolysins [1,2] are toxins produced by a variety of Gram-positive bacteria and are characterized by their ability to lyse cholesterol-containing membranes, their reversible inactivation by oxidation and their capacity to bind to cholesterol. The sequences of some of these toxins is currently known:
- Alveolysin (gene alv) from Bacillus alvei.
- Ivanolysin (gene ilo) from Listeria ivanovii.
- Listeriolysin O (gene hlyA) from Listeria monocytogenes.
- Perfringolysin O (theta-toxin) (gene pfo) from Clostridium perfringens.
- Pneumolysin (gene ply) from Streptococcus pneumoniae.
- Seeligeriolysin (gene lso) from Listeria seeligeri.
- Streptolysin O (gene slo) from Streptococcus pyogenes.
All these proteins contain a single cysteine residue, located in their C-terminal section, which has been shown [3] to be essential for the binding to cholesterol. This cysteine is located in a highly conserved region that can be used as a signature pattern.
Last update:October 1993 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Alouf J.E. Geoffroy C. |
| Source | (In) Bacterial proteins toxins, pp 165-171, Alouf J.E., Ferenbach F.J., Free J.H., Jeljaszewicz J., Ed., Academic Press, London, (1984). |
| 2 | Authors | Geoffroy C. Mengaud J. Alouf J.E. Cossart P. |
| Source | J. Bacteriol. 172:7301-7305(1990). |
| 3 | Authors | Iwamoto M. Ohno-Iwashita Y. Ando S. |
| Title | Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens. | |
| Source | Eur. J. Biochem. 167:425-430(1987). | |
| PubMed ID | 2888650 |
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