The antibacterial activity of various saturated and unsaturated fatty acids against several oral pathogens.

The antibacterial activity of various saturated fatty acids (SFA) and unsaturated fatty acids (USFA) against different oral pathogens which are implicated in the cause of dental caries, stomatitis, gingivitis, and periodontitis was examined. The saturated fatty acids Pa, StA and ArA, and the unsaturated w-7 fatty acids PLA and w-9 fatty acids OA showed either none to low antimicrobial activity against all of the 12 oral pathogenic strains used in this study. In contrast, the w-3 PUFAs, ALA, SDA, EPA and DHA, and the w-6 PUFAs, LA, GLA, and AA showed considerable antimicrobial activity against 8, 7, 6 and 5 strains, and 6, 10 and 5 strains, respectively. In particular, the w-3 and w-6 PUFAs showed strong antimicrobial activity against Porphyromonas gingivalis KCTC 381, the cause of periodontitis, and against Aggregatibacter segnis KCTC 5968, Fusobacterium nucleatum subsp. Polymorphum KCTC 5172 and Prevotella intermedia KCTC 25611, all organisms implicated in the cause of gingivitis. To date, no bacterial resistance to free fatty acids has been encountered and no resistance phenotype has emerged. Therefore, these results suggest that PUFAs may be useful in the development of therapeutic agents for oral diseases, and in particular, in the development of agents that have minimal side effects and against which there is no bacterial resistance.

Exploration of receptor binding of Bacillus thuringiensis toxins

Wild type and mutant toxins of Bacillus thuringiensis delta-endotoxins were examined for their binding to midgut brush border membrane vesicles (BBMV). CryIAa, CryIAb, and CryIAc were examined for their binding to Gypsy moth (Lymantria dispar) BBMV. The binding of CryIAa and CryIAc was directly correlated with their toxicity, while CryIAb was observed to have lower binding than expected from its toxicity. The latter observation confirms the observation of Wolfersberger (1990). The "rule" of reciprocity of binding and toxicity is apparently obeyed by CryIAa and CryIAc, but broken by CryIAb on L. dispar. Alanine substitutions were made in several positions of the putative loops of CryIAa to test the hypothesis that the loops are intimately involved in binding to the receptor. The mutant toxins showed minor shifts in heterologous binding to Bombyx mori BBMV, but not enough to conclude that the residues chosen play critical roles in receptor binding.