Degradation of plasma proteins by the trypsin-like enzyme of Porphyromonas gingivalis and inhibition of protease activity by a serine protease inhibitor of human plasma.
The interaction between Porphyromonas gingivalis culture supernatant and human serum was examined. Hydrolysis of the major serum proteins was thiol-dependent and correlated with the trypsin-like activity of the sample. Transferrin and IgG light chains were less susceptible to degradation than albumin and IgG heavy chains and partially degraded IgG retained antigen-binding capability. Serum inhibited the trypsin-like activity in a fluorimetric assay. The inhibition was shown to be independent of the level of IgG antibody reactive with whole cells of P. gingivalis. Purified preparations of antithrombin III, a serine protease inhibitor, but not alpha 1-antitrypsin nor alpha 2-macroglobulin inhibited the trypsin-like activity in the fluorometric assay.
Fishburn
C S
CS
MRC Dental Research Unit, London Hospital Medical College.
Slaney
J M
JM
Carman
R J
RJ
Curtis
M A
MA
D000942:Antigens, Bacterial / Q000276:immunology; D001425:Bacterial Outer Membrane Proteins / Q000276:immunology / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D006801:Humans; D010510:Periodontal Diseases / Q000097:blood / Q000382:microbiology; D016966:Porphyromonas gingivalis / Q000201:enzymology* / Q000472:pathogenicity; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000097:blood* / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism*
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001798:Blood Proteins; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; D014357:Trypsin; D003545:Cysteine