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Cholera toxin (CT), the enterotoxin secreted by Vibrio cholerae classical as well as El Tor biotypes, is the major causative agent of the acute diarrheal disease of humans. CT and the Escherichia coli heat labile enterotoxin (LT),are structurally and immunologically highly homologous,seeing that they belong to the same enterotoxin family (de Haan and Hirst, 2004; Spangler, 1992; Vanden Broeck et al., 2007). Both are oligomeric proteins of the A-B type. CT is composed of one A or activating subunit (CT-A Mr 27,400), which consists of two distinct polypeptide chains CT-A1 (Mr 22,000) and CT-A2 (Mr 5,400), linked by a single disulfide bridge, and 5 identical B subunits (Mr 11,600) arranged in a ring like configuration (CT-B).

Brefeldin A and Exo1 Completely Releave the Block of Cholera Toxin Action by a Dipeptide Metalloendoprotease Substrate