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Porphyromonas gingivalis proteinases as virulence factors in the development of periodontitis
Author(s) -
Travis J.,
Pike R.,
Imamura T.,
Potempa J.
Publication year - 1997
Publication title -
journal of periodontal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.31
H-Index - 83
eISSN - 1600-0765
pISSN - 0022-3484
DOI - 10.1111/j.1600-0765.1997.tb01392.x
Subject(s) - porphyromonas gingivalis , virulence , periodontitis , microbiology and biotechnology , virulence factor , chronic periodontitis , medicine , biology , dentistry , genetics , gene
Porphyromonas gingivalis contains exceedingly high concentrations of cysteine proteinases with trypsin‐like activity which have been implicated as virulence factors in adult‐onset periodontitis. These enzymes, referred to as gingipains, cleave protein and peptide substrates after arginine (gingipain R) and lysine residues (gingipain K), and it has been found that neither is easily inhibited by host proteinase inhibitors. Examination of the properties of each proteinase clearly indicates a role(s) for both in the dysregulation of a number of normally tightly controlled pathways. The effects of such uncontrolled proteolysis are the development of edema (kallikrein/kinin pathway activation by gingipain R), neutrophil infiltration (complement pathway activation by gingipain R), and bleeding (degradation of fibrinogen by gingipain K). Since three of the major hallmarks of periodontitis involve increased crevicular flow, neutrophil accumulation at infected sites and bleeding on probing, it seems likely that both P. gingivalis ‐derived proteinases are important virulence factors in the development of periodontal disease.