Cytolytic toxin

In contradistinction to site-specific molecules there are other toxins which, in a sense, create their own specificity. Thus ionophore toxins, by opening up the cell membrane to sodium and calcium ions, create their own specificity. Prime examples of this are found in cytolytic toxins in general, and jellyfish toxins and palytoxin in particular. 

In terms of their mode of action, insecticides fall into seven classes physical toxicants, protoplasmic poisons, nerve poisons, metabolic inhibitors, cytolytic toxins, muscle poisons, and alkylating agents. 

Cytoplasmic, Neurological, and Muscular Poisons, Metabolic Inhibitors, Cytolytic Toxins, and Alkylating Agents... 

Alouf JE, Geoffrey C (1991) The family of the antigenically-related, cholesterolbinding ("sulphydryl-activated") cytolytic toxins. In Alouf JE, Freer JH (ed) Sourcebook of bacterial protein toxins. Academic Press Ltd, p. 147-186. 

Gazit E, Shai Y (1993) Structural characterization, membrane interaction, and specific assembly within phospholipid membranes of hydrophobic segments brom bacillus thuringiensis var. israelensis cytolytic toxin. 

Most exotoxins fall into one of three categories on the basis of their structure and activities. These are the A-B toxins, the cytolytic toxins and the superantigen toxins. The A-B toxins consist of a B subunit that binds to a host cell receptor, covalently bound to the A subunit that mediates the enzymic activity responsible for toxicity. Most exotoxins (e.g. diphtheria toxin, cholera toxin) are of the A-B category. The cytolytic toxins such as haemolysins and phospholipases do not have separable A and B... 

Cytolytic toxin produced by the Sea Pink sea anemone (Metridium senile). Produce 33 nm diameter ring like structures in cell membranes. 

Toxins that act directly on cell membranes, called cytolytic toxins, disturb and ultimately kill the target cells. Produced by many organisms (e.g., bacteria, fungi, plants, fish, and snakes), cytolytic toxins may cause damage in several ways. For example, streptolysin O (67,000 D), produced by the bacterium Streptococcus pyogenes, causes pores to form in the target cell membranes. Affected cells are rapidly lysed because the cell membrane is much more permeable to ions such as Na+. Streptolysin O is believed to cause some of the damage in rheumatic fever. 

Gilmore MS, Segarra RA, Booth MC, Bogie CP, Hall LR, Clewell DB (1994) Genetic structure of 1iie Enterococcus faecalis plasmid pADl-encoded cytolytic toxin system and its relationship to lantibiotic determinants.) Bacteriol 176 7335-7344... 

Farrand AJ, LaChapelle S, Hotze EM, Johnson AE, Tweten RK. Only two amino adds are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sd USA. 2010 107(9) 4341-4346. 

Bernheimer and Avigad 285) examined seven kinds of sea anemones for the presence of cytolytic toxins. Tealia lofotensis and Epiactis prolifera yielded especially powerful preparations, whereas the extracts of the other species showed weaker cytolytic activity. Natural-abundance NMR studies have been performed on toxic polypeptides. These studies of APA and ATX II indicated that their overall conformation was very similar 286). 

Varanda, W., and A. Finkelstein Ion and Nonelectrolyte Permeability Properties at Channels Formed in Planar Lipid Bilayer Membranes by the Cytolytic Toxin from the Sea Anemone Stoichactis helianthus. J. Membrane Biol. 55, 203 (1980). 

MaCek, P., and D. Lebez Kinetics of Hemolysis Induced by Equinatoxin, a Cytolytic Toxin from the Sea Anemone Actinia equina. Effect of Some Ions and pH. Toxicon 19, 233 (1981). 

Du, J., B.H. Knowles, J. Li, and D.J. Ellar. 1999. Biochemical characterization of Bacillus thuringiensis cytolytic toxins in association with a phospholipid bilayer. Biochem. J. 338 185-193. 

Gazit, E., N. Burshtein, D.J. Ellar, T. Sawyer, and Y. Shai. 1997. Bacillus thuringiensis cytolytic toxin associates specifically with its synthetic helices A and C in the membrane bound state. Implications for the assembly of oligomeric transmembrane pores. Biochemistry 36 15546-15554. 

Manceva, S.D., M. Pusztai-Carey, P.S. Russo, and P. Burko. 2005. A detergent-like mechanism of action of the cytolytic toxin Cytl A from Bacillus thuringiensis var. israelensis. Biochemistry 44 589-597. 

Macek, P. (1992) Polypeptide cytolytic toxins from sea anemones Actinaria). FEMS Microbiol. Letters, 105,121-129. 

Samejima, Y, Yanagisawa, M., Aoki-Tomomatsu, Y, Iwasaki, E., Ando, J., and Mebs, D. (2000) Aminoacid sequence studies on cytolytic toxins from sea anemone Heteractis magnifica, Entacmea quadricolor and Stichodactyla mertensii (Anthozoa). Toxicon, 38, 259-264. 

Sencic, L. and Macek, P. (1990) New method for isolation of venom from the sea anemone Actinia cari. Purification and characterization of cytolytic toxins. Comp. Biochem. Physiol, 97B, 687-693. 

Turk, T. (1991) Cytolytic toxins from sea anemones. J. Toxicol. Toxin Rev., 10, 223-262. 

Shier, W. T., Activation of self-destmction as a mechanism of action for cytolytic toxins. In Natural Toxins, D. Eaker and T. Wadstrom, eds. Permagon Press, Oxford and New York, pp. 193-200. 

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