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J Biol Chem, Vol. 273, Issue 33, 21225-21231, August 14, 1998
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From the Departments of The oral anaerobic bacterium Porphyromonas
gingivalis, a major pathogen of advanced adult periodontitis,
produces a novel class of cysteine proteinases in both cell-associated
and secretory forms. A lysine-specific cysteine proteinase
(Lys-gingipain, KGP), as well as an arginine-specific cysteine
proteinase (Arg-gingipain), is a major trypsin-like proteinase of the
organism. Recent studies indicate that the secreted KGP is implicated
in the destruction of periodontal tissue and the disruption of host
defense mechanisms. In this study, we have constructed a KGP-deficient
mutant to determine whether the cell-associated KGP is important for
pathophysiology of the organism. Although the mutant retained the
strong ability to disrupt the bactericidal activity of
polymorphonuclear leukocytes, its hemagglutination activity was reduced
to about one-half that observed with the wild-type strain. More
important, the mutant did not form black-pigmented colonies on blood
agar plates, indicating the defect of hemoglobin adsorption and heme
accumulation. Immunoblot analysis showed that the expression of a
19-kDa hemoglobin receptor protein, which is thought to be responsible
for hemoglobin binding by the organism, was greatly retarded in this
mutant. The mutant also showed a marked decrease in the ability to
degrade fibrinogen. These results suggest the possible involvement of
KGP in the hemoglobin binding and heme accumulation of the organism and
in the bleeding tendency in periodontal pockets.
Pharmacology and
¶ Microbiology, Kyushu University Faculty of Dentistry,
Higashi-ku, Fukuoka 812-8582, Japan
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