Inactivation of human serum bactericidal activity by a trypsinlike protease isolated from Porphyromonas gingivalis.
A protease was isolated from an outer membrane vesicle preparation of Porphyromonas gingivalis ATCC 33277 and assessed for its ability to inactivate the bactericidal activity of normal human serum. The enzyme, which was activated by reducing agents, was found to be a trypsinlike protease with a molecular mass of approximately 80 kDa. Prior to being tested in the bactericidal assay, pooled human serum was preincubated with the partially purified enzyme. Under conditions in which the trypsinlike protease was activated, a strong reduction of the serum bactericidal activity against Capnocytophaga ochracea was noted. On the other hand, no reduction of the bactericidal action of serum was observed when the serum-protease mixture was preincubated in the presence of an inhibitor of the enzyme. As determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the protease was shown to degrade immunoglobulins G and M as well as complement factor C3. This study confirms the previous hypothesis that the proteases of P. gingivalis can interfere with the protective action of human serum.
Grenier
D
D
Département de Santé Buccale, Faculté de Médecine Dentaire, Université de Montréal, Québec, Canada.
D001770:Blood Bactericidal Activity / Q000187:drug effects*; D010450:Endopeptidases / Q000302:isolation & purification / Q000633:toxicity*; D006801:Humans; D066298:In Vitro Techniques; D016966:Porphyromonas gingivalis / Q000201:enzymology* / Q000472:pathogenicity
D010450:Endopeptidases