Consumption of Peptide-derived Arginine by a Periodontopathogenic Bacterium, Porphyromonas gingivalis

Abstract The specificity of amino acid consumption by Porphyromonas gingivalis , well known as an important pathogen of adult periodontitis, is described. P. gingivalis is an asaccharolytic, black-pigmented and gram-negative anaerobe and produces several types of proteases including cysteine proteases such as arg-gingipain and trypsin-like enzyme. This suggests that arginine is a possible energy source for its growth. When P. gingivalis was grown anaerobically in brain–heart infusion broth, several free amino acids such as lysine, glycine and glutamic acid increased in the culture supernatant with the bacterial growth; but free arginine increased first and then started to decrease after the early log phase. Citrulline and ornithine increased to late log phase in contrast to the decrease of arginine. The total arginine in the medium decreased steadily with the growth of P. gingivalis . In relation to the arginine consumption, cell extracts of P. gingivalis clearly demonstrated enzyme activities for the arginine deiminase pathway and adenosine triphosphate production. The arginine deiminase pathway was also presumed from the presence of putative homologue corresponding to the other bacterial arginine deiminase pathway relating enzymes in the unfinished P. gingivalis W83 genome. These results suggest that P. gingivalis catabolizes arginine which is released from proteins and/or peptides by several types of proteases, and obtains energy through the arginine deiminase pathway.