Bacteroides fragilis are both key commensals and important human pathogens. Particular strains of B. fragilis, termed enterotoxigenic B. fragilis (ETBF), are recently identified enteric pathogens of children and adults. These strains are distinguished by secretion of a 20kDa metalloprotease toxin (B. fragilis toxin or BFT), the first recognized and only established toxin to date for B. fragilis. Three isotypes of BFT are encoded by distinct bft loci contained within a 6kb chromosomal region unique to ETBF strains termed the B. fragilis pathogenicity island (BfPAI). Experimental studies have suggested that the cellular target for BFT is E-cadherin, the primary protein of the zonula adherens. It is postulated that BFT cleavage of E-cadherin is critical in precipitating the intracellular events culminating in the two established activities for BFT; namely, stimulation of secretion in ligated intestinal segments in several animal species and alteration of cellular morphology only in epithelial cells that retain the ability to polarize and form a tight junctional complex. Future studies will be directed to characterizing in greater detail both the molecular genetics of the BFT toxin and the precise steps in its cellular mechanism of action.