Description
Escherichia coli heat-labile enterotoxin (LT) is the causative agent of traveler's diarrhea, and it is also responsible for the deaths of hundreds of thousands of children per year in developing countries. LT is highly homologous in sequence, structure and function to cholera toxin (CT). Both toxins attack intestinal epithelial cells via specific binding to the branched pentasaccharide of ganglioside GM1 at the cell surface. LT is a plasmid-encoded, high molecular weight toxin, the crystalline structure of which revealed that it is composed of one A subunit (LTA) (27 kDa) and five non-covalently associated B subunits (LTB) (11.6 kDa each) forming a ring-like pentamer. The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. The B chain has a membrane binding function. A receptor binding antagonist which blocked the interaction of LT and CT with cell surface GM1 would potentially constitute a prophylactic drug conferring protection both against the severe effects of cholera itself and against the milder but more common disease caused by LT.
Bioinformatics
| Alternate Names |
- eltB
- ltpB
- LTP B
- LTH B
- LTB
- LT B
- Heat labile enterotoxin B chain
- eltB
- ltpB
- LTP B
- LTH B
- LTB
- LT B
- Heat labile enterotoxin B chain
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