LTA and LTB

Escherichia coli heat-resistant enterotoxin (LT) has been proven to be a potent mucosal immune adjuvant, but its toxicity has limited its use. The complete LT molecule consists of 1 A subunit (LTA) and 5 B subunits (m). A subunit has the activity of adp-ribosyltransferase and is also the site of toxin toxicity. B subunit can bind to GMl on the surface of mammalian cells. Many studies confirmed that both m and LTB had mucosal immune adjuvant activity, in which LTB mucosal immune adjuvant activity was stronger than the cholera toxin B subunit (CTB). In recent years, the LTA 63th silk after mutation into amino acid lysine, the intestinal toxicity declined obviously, but still retain adjuvant activity and call the mutant LTKA63 down. However, the LTA or LTKA63 adjuvant active up to now, the mechanism of restructuring LT & offer 3 (d guanidine A63) and LTB (rLTB) enhance different antigen immune protection effect also needs to be more research materials confirmed.