Abstract
Cysteine protease and hemagglutinin activities of Porphyromonas gingivalis have been implicated as virulence factors in periodontitis. In addition, a close structural relationship between these factors has been suggested. In order to examine the molecular basis for such a relationship, we constructed an isogenic mutant, G-102, of P. gingivalis 381 deficient in Arg-gingipain cysteine protease activity. The mutant displayed not only reduced protease activity but also significantly reduced hemagglutination activity compared with the wild-type strain. Therefore, this investigation provided genetic evidence for the recently proposed structural relationship between Arg-gingipain and the hemagglutinin activity of P. gingivalis strains.
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