Glycosulfatase activity of Porphyromonas gingivalis a bacterium associated with periodontal disease.
Porphyromonas gingivalis, a bacterium implicated in the pathogenesis of periodontal disease, was found to elaborate an extracellular glycosulfatase enzyme. Upon purification by low temperature acetone fractionation, an active enzyme at 60% acetone was obtained which on SDS-PAGE gave a protein band of 37kDa. The glycosulfatase effectively caused desulfation of galactosyl- and lactosylceramide sulfates (pH 5.0) which contain the sulfate ester groups at C-3 of galactose, a well as proteoglycans (pH 5.7-6.2) of gingival tissue which are rich in N-acetylgalactosamine-4-sulfate, but not the sulfated salivary mucin with the sulfate groups at C-6 of galactose and C-6 of N-acetylglucosamine. The results demonstrate for the first time that P. gingivalis displays glycosulfatase activity and that the disruptive action of this enzyme may be a major factor in the etiology of periodontal disease.
Research Center, New Jersey Dental School, University of Medicine and Dentistry of New Jersey, Newark 07103-2400.
B L
BL
Slomiany
V L
VL
Murty
J
J
Piotrowski
Y H
YH
Liau
A
A
Slomiany
D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D006028:Glycosphingolipids / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D016966:Porphyromonas gingivalis / Q000201:enzymology*; D011509:Proteoglycans / Q000378:metabolism; D013429:Sulfatases / Q000302:isolation & purification / Q000378:metabolism*
D003470:Culture Media; D006028:Glycosphingolipids; D011509:Proteoglycans; D013429:Sulfatases; C022758:glycosulphatase