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.
Slomiany
B L
BL
Research Center, New Jersey Dental School, University of Medicine and Dentistry of New Jersey, Newark 07103-2400.
Murty
V L
VL
Piotrowski
J
J
Liau
Y H
YH
Sundaram
P
P
Slomiany
A
A
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