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J Biol Chem, Vol. 274, Issue 18, 12245-12251, April 30, 1999

Purification and Characterization of a Novel Cysteine Proteinase (Periodontain) from Porphyromonas gingivalis
EVIDENCE FOR A ROLE IN THE INACTIVATION OF HUMAN ₁-PROTEINASE INHIBITOR

Daniel Nelson, Jan Potempa, Tomasz Kordula^§, and James Travis

From the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 and the Departments of  Microbiology and Immunology and ^§ Animal Biochemistry, Jagiellonian University, 31-120 Krakow, Poland

Periodontal disease is characterized by inflammation of the periodontium manifested by recruitment of neutrophils, which can degranulate, releasing powerful proteinases responsible for destruction of connective tissues, and eventual loss of tooth attachment. Although the presence of host proteinase inhibitors (serpins) should minimize tissue damage by endogenous proteinases, this is not seen clinically, and it has been speculated that proteolytic inactivation of serpins may contribute to progression of the disease. A major pathogen associated with periodontal disease is the Gram-negative anaerobe Porphyromonas gingivalis, and in this report, we describe a novel proteinase that has been isolated from culture supernatants of this organism that is capable of inactivating the human serpin, ₁-proteinase inhibitor, the primary endogenous regulator of human neutrophil elastase. This new enzyme, referred to as periodontain, belongs to the cysteine proteinase family based on inhibition studies and exists as a 75-kDa heterodimer. Furthermore, periodontain shares significant homology to streptopain, a proteinase from Streptococcus pyogenes, and prtT, a putative proteinase from P. gingivalis. Clearly, the presence of this enzyme, which rapidly inactivates ₁-proteinase inhibitor, could result in elevated levels of human neutrophil elastase clinically detected in periodontal disease and should be considered as a potential virulence factor for P. gingivalis.

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