Identification of Epitopes of the Receptor Binding Subunit of Cholera Toxin by Synthetic Peptide and CBIB Approaches
Cholera toxin (CT) and related diarrheagenic heat-labile enterotoxins (LTs) are produced, among others, by strains of Vibrio cholerae as well as strains of Escherichia coli of human (H) and porcine (P) origin (reviewed in Finkelstein, 1988). These enterotoxins are structurally, immunologically and functionally related. All CT-related toxins consist of a homopentamer receptor-binding B-subunit protein and an enzymatically active A-subunit. The B-subunit proteins, designated as CT-B-1 and CT-B-2 (from classical and E1 Tor biotype strains of V. cholerae 569B and 3083, respectively) as well as H-LT-B and P-LT-B (from E. coli strains) bind to GM1 ganglioside on the surface of target cells. Receptor-binding is essential for the internalization and the intracellular activity of the A-subunit protein. Identification of the epitopes of the immunodominant CT-related B-subunit proteins, particularly those that are involved in the receptor-binding process, is of great interest for vaccine development. In this report we describe two different approaches that we have taken to analyze the epitopic regions of CT-B-1.
KeywordsSynthetic Peptide Cholera Toxin Human Seron Conformational Epitope Epitopic Region
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