Failure of Bacteroides gingivalis W83 to accumulate bound C3 following opsonization with serum.

Our previous studies have demonstrated that strains of Bacteroides gingivalis are capable of proteolytic degradation and inactivation of complement proteins including the third component of complement C3. Since a crucial step in the ability of complement to control bacterial infections is the binding of C3 fragments to the bacterial surface with subsequent enhancement of phagocytosis, further examination of the importance of the proteolytic capacity of Bacteroides in interactions with complement proteins was carried out by quantitating the amount of C3 bound to two proteolytic Bacteroides gingivalis strains. Pooled normal human serum (NHS) containing 125I-C3 was incubated with strains of B. gingivalis (W83 and ATCC 33277) and the non-proteolytic pathogen A. actinomycetemcomitans strain Y4, and samples of the reaction mixtures were removed at various time intervals for determination of bound C3. B. gingivalis 33277 bound only half the number of C3 molecules as did A. actinomycetemcomitans, while B. gingivalis W83 bound very little C3. A large increase in the number of C3 molecules bound to B. gingivalis W83 was noted in assays carried out in the presence of the protease inhibitor TLCK, indicating that bacterial proteases may be responsible for the lack of binding of C3 to strain W83. TLCK treatment modestly increased the accumulation of C3 on strain 33277, but had no effect on A. actinomycetemcomitans. Analysis of 125I-C3 in supernatants from reaction mixtures of strain 33277, W83, or a proteolytic strain of B. intermedius demonstrated no qualitative differences in the C3 fragments amongst the tested strains or in the presence or absence of TLCK.(ABSTRACT TRUNCATED AT 250 WORDS)