Serum inhibition of Porphyromonas gingivalis protease in the dog, cat and sheep - A preliminary study

摘要

The Gram negative anaerobic bacterium Porphyromonas gingivalis is implicated in human (Slots et al., 1986) canine (Allaker et al., 1997c), feline (Love et al., 1989) and ovine periodontitis (Ismaiel et al., 1989). Evidence suggests that the survival and growth of P. gingivalis depends upon hydrolytic enzyme actiw ity. The major extra-cellular arginine-specific proteases of P. gingivalis, arg-gingipains (Rgp A & B), are considered to be potential virulence determinants in chronic periodontal disease of man. The RgpA enzyme is composed of catalytic (#alpha#) and adhesin (#beta#) domains, and is encoded by the gene rgpA (Aduse-Opoku et al., 1995). The gene encoding the cs region of the rgpA locus is conserved within P. gingivalis from man (Allaker et al., 1997a). It is plausible that equivalent genes are conserved in P. gingivalis from animals. However, as a consequence of evolutionary pressure on P. gingivalis in different hosts, genetic differences with corresponding differences in phenotype and pathogenic potential may have resulted.