Glycosulfatase activity of Helicobacter pylori toward gastric mucin.
A glycosulfatase activity toward sulfated gastric mucus glycoprotein was identified in the extracellular material elaborated by H. pylori, a bacteria implicated in the etiology of gastric disease. Upon acetone precipitation, an active enzyme fraction at 64% acetone was obtained which on SDS-PAGE gave a major 30kDa protein band. The H. pylori glycosulfatase exhibited maximum activity (314.8 pmol/mg protein/h) at pH 5.7 in the presence of Triton X-100 and CaCl2, and was capable of removal of the sulfate ester groups situated at C-6 of N-acetylglucosamine, galactose and glucose. However, the enzyme was ineffective toward galactosylceramide and lactosylceramide sulfates which contain the sulfate ester group on C-3 of galactose. The results suggest that H. pylori is capable of overcoming the interference by sulfated mucus glycoprotein with its colonization of gastric mucosa.
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
P
P
Sundaram
A
A
Slomiany
D005752:Gastric Mucins / Q000378:metabolism*; D005753:Gastric Mucosa / Q000382:microbiology*; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D016480:Helicobacter pylori / Q000201:enzymology*; D006801:Humans; D013272:Stomach Diseases / Q000209:etiology; D013379:Substrate Specificity; D013429:Sulfatases / Q000378:metabolism*
D005752:Gastric Mucins; D006023:Glycoproteins; C047874:gastric mucus glycoproteins; D013429:Sulfatases