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Heat-stable enterotoxins are secretory peptides produced by some bacterial strains. These peptides keep their 3D structure and remain active at 100oC. Different STs recognize distinct receptors on the cell surface and thereby affect different intracellular signaling pathways. For example, STa enterotoxins bind and activate membrane-bound guanylate cyclase, which leads to the intracellular accumulation of cyclic GMP and downstream effects on several signaling pathways. These events lead to the loss of electrolytes and water from intestinal cells.
Additional recommended knowledge
Members of heat-stable enterotoxin B family assume a helical secondary structure, with two alpha helices forming a disulphide cross-linked alpha-helical hairpin. The disulphide bonds are crucial for the toxic activity of the protein, and are required for maintenance of the tertiary structure, and subsequent interaction with the particulate form of guanylate cyclase, increasing cyclic GMP levels within the host intestinal epithelial cells.
This article includes text from the public domain Pfam and InterPro IPR015160
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Heat-stable_enterotoxin". A list of authors is available in Wikipedia.|