Brefeldin A and Exo1 completely releave the block of cholera toxin action by a dipeptide metalloendoprotease substrate


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

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Authors & affiliation: 
Davy Vanden Broeck and Marc J.S. De Wolf International Centre for Reproductive Health, Ghent University, Ghent, Belgium
Staff Members: 
Published In: 
booktitle: Cholera. p.153-176 editor Sivakumar Joghi Thatha Gowder
Publication date: 
Tuesday, May 6, 2014