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J. Bacteriol., 05 1996, 2876-2882, Vol 178, No. 10
RN Pike, J Potempa, W McGraw, TH Coetzer and J Travis
Adhesins from oral bacteria perform an important function in colonizing
target tissues within the dentogingival cavity. In Porphyromonas gingivalis
certain of these adhesion proteins exist as a complex with either of two
major proteinases referred to as gingipain R (arginine- specific gingipain)
and gingipain K (lysine-specific gingipain) (R. N. Pike, W. T. McGraw, J.
Potempa, and J. Travis, J. Biol. Chem. 269:406- 411, 1994). With specific
proteinase inhibitors, it was shown that hemagglutination by either
proteinase-adhesin complex could occur independently of proteinase
activity. Significantly, low concentrations of fibrinogen, fibronectin, and
laminin inhibited hemagglutination, indicating that adherence to these
proteins and not the hemagglutination activity was a primary property of
the adhesin activity component of complexes. Binding studies with gingipain
K and gingipain R suggest that interaction with fibrinogen is a major
function of the adhesin domain, with dissociation constants for binding to
fibrinogen being 4 and 8.5 nM, respectively. Specific association with
fibronectin and laminin was also found. All bound proteins were degraded by
the functional proteinase domain, with gingipain R being more active on
laminin and fibronectin and gingipain K being more effective in the
digestion of fibrinogen. Cumulatively, these data suggest that gingipain R
and gingipain K, acting as proteinase-adhesin complexes, progressively
attach to, degrade, and detach from target proteins. Since such complexes
appear to be present on the surfaces of both vesicles and membranes of P.
gingivalis, they may play an important role in the attachment of this
bacterium to host cell surfaces.
Copyright © 1996, American Society for Microbiology
Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis
Biochemistry Department, University of Natal, Pietermaritzburg, South Africa.
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