Abstract
The basic structure and biological function of cholera toxin (CT) and heat-labile toxin of enterotoxigenic Escherichia coli (LT), which induces diarrhea in humans, are similar. Both CT and LT act as adjuvants for the enhancement of mucosal and serum antibody responses to the mucosally co-administered protein antigen. CT acts as an adjuvant by inducing IL-4-dependent Th2 cytokine responses, which provide help for antigen-specific secretory IgA (S-IgA) as well as serum IgGl, IgA and IgE antibody responses. On the other hand, LT induces Th1- and partly IL-4-independent Th2-type cells with subsequent serum IgGl, IgG2a and mucosal S-IgA responses. Nontoxic mutant CT (mCT) and the chimeric molecule that combine the A subunit of mCT with the B subunit of LT (mCTA/LTB), like nCT, act as mucosal adjuvants and induce mucosal IgA and systemic IgG and IgA antibody responses. These studies indicate that ADP- ribosyltransferase activity can be separated from the adjuvant properties of CT and LT. Further, those nontoxic enterotoxin derivatives should be considered as candidate mucosal adjuvants for vaccinating humans.
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