Cholera toxin, a main enterotoxin, interacts with G proteins and increases cyclic AMP in the intestinal lining to open ion channels. As ions flow into the intestinal lumen (lining), body fluids (mostly water) flows out of the body due to osmosis leading to massive diarrhea as the fluid is expelled from the body. Cholera toxin is a complex consisting of one molecule of A subunit (27.2 kD) and 5 molecules of B subunits (11.6 kD). After secretion, A subunit is proteolytically processed into A1 (22 kD) and A2 (5 kD) subunits which are held together by a disulfide bond. The toxin adsorbs to GM1 ganglioside on the surface of target cells by the B subunit and the A subunit is dissociated from the B subunit during penetration. The A subunit constitutively activates adenyl cyclase activity of α subunit of Gs (a kind of GTP-binding protein).
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