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Double mutant Escherichia coli heat-labile toxin (dmLT), also known as LT(R192G/L211A), is a genetically detoxified derivative of the wild-type enterotoxigenic Escherichia coli (ETEC) heat-labile enterotoxin (LT). It is designed for use as a potent mucosal and parenteral vaccine adjuvant. The molecule is an AB5-type protein consisting of an enzymatically active A subunit non-covalently associated with a pentameric B subunit. By introducing two point mutations in the A subunit (R192G and L211A), the ADP-ribosyltransferase activity is significantly reduced, eliminating enterotoxicity while preserving its strong adjuvant properties. dmLT enhances antigen-specific immune responses, including Th1, Th2, and Th17 cellular responses, as well as systemic IgG and mucosal IgA antibody production. It is being developed for use in vaccines against enteric pathogens such as ETEC, polio, and other infectious diseases.
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