Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins

R. Pike, W. McGraw, J. Potempa, J. Travis

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Abstract

Porphyromonas gingivalis contains many virulence factors that have been implicated as participants in the progression of periodontal disease. It has been shown to produce proteinases of 'trypsin-like' specificity in a number of molecular forms, but previous work in our laboratory resulted in the purification of a major arginine-specific cysteine proteinase, gingipain, which contradicted this supposed specificity. In this study, separate proteinases with arginine and lysine specificity were isolated from a high molecular mass fraction of the P. gingivalis culture fluid. The arginine- specific enzyme was found, by amino acid sequencing studies, to be a high molecular mass form of gingipain, formed by the 50-kDa gingipain noncovalently complexed with 44-kDa binding proteins, subsequently identified as hemagglutinins. The 60-kDa lysine-specific proteinase, referred to as Lys- gingipain, was also found to have one of these hemagglutinins complexed with it in the same manner. Lys-gingipain was found to be a cysteine proteinase with optimal activity and stability at pH 8.0-8.5 and was extensively characterized in terms of its specificity and activation characteristics. The proteinase-hemagglutinin complexes may be important in the uptake of hemin, a vital metabolite for P. gingivalis, via hemagglutination and subsequent hemolysis of erythrocytes.

Original languageEnglish
Pages (from-to)406-411
Number of pages6
JournalJournal of Biological Chemistry
Volume269
Issue number1
Publication statusPublished - 1 Jan 1994
Externally publishedYes

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