Arylaminopeptidase activities of oral bacteria

Protease and peptidase enzymes are thought to play a role in the virulence of many oral organisms, especially those associated with periodontal diseases. In order to evaluate the peptidases of periodontopathogens, we compared the arylaminopeptidase activities of Bacteroides gingivalis with those of other oral and non-oral bacteria. Sixty-three bacterial strains representing the prominent cultivable organisms in human periodontal pockets were tested, including representatives of the black-pigmented Bacteroides, Actinobacillus, Actinomyces, Campylobacter, Capnocytophaga, Eikenella, Fusobacterium, Haemophilus, Lactobacillus, Streptococcus, and Veillonella species. Each micro-organism was examined for its ability to hydrolyze 18 synthetic substrates of beta-naphthylamide derivatives of amino acids, dipeptides, and tripeptides. Quantitation of the enzyme activity was accomplished by colorimetric measurement of the amounts of released beta-naphthylamines. N-CBz-glycyl-glycyl-L-arginine-beta-naphthylamide was readily cleaved by B. gingivalis, but slightly or not at all by the other oral strains tested. L-arginine-beta-naphthylamide was cleaved by B. gingivalis, Capnocytophaga species, and Streptococcus species, but not readily by the other Bacteroides strains. Some dipeptide substrates tested, such as glycyl-L-arginine- and glycyl-L-proline-beta-naphthylamide, were strongly cleaved by B. gingivalis and weakly cleaved by other Bacteroides strains. Since high levels of N-CBz-glycyl-glycyl-L-arginyl-aminopeptidase activity are characteristic of B. gingivalis, its measurement may be valuable in the identification of this organism in clinical samples as an aid in diagnosis and monitoring of periodontal infections. Furthermore, this and other aminopeptidases produced by B. gingivalis and other oral organisms may play a role in the tissue destruction seen in periodontal disease.