The urease enzymes of Campylobacter pylori and a related bacterium.
The urease enzyme of Campylobacter pylori was studied and compared with that of a related spiral-shaped bacterium, St1, isolated from the rodent ileum. Both bacteria possessed constitutive urease enzymes with activities up to 20-70 times that of Proteus vulgaris. This activity was retained on SDS-polyacrylamide gels. A major catalytic subunit of mol. wt 300,000 was located for all (six) strains of C. pylori subjected to SDS-PAGE whereas St1 had two active forms of mol. wts 140,000 and 150,000. Western-blot analysis indicated the presence of anti-urease antibodies in the sera of patients with C. pylori-associated gastritis. The response to C. pylori urease was not strain-specific but no cross-reactivity was detected between the C. pylori enzyme and that of St1. The very high urease activity of these bacteria is likely to be important in colonisation of the host. Possession of glutamate dehydrogenase activity by both organisms suggests that one role of the urease may be to assimilate the available urea nitrogen. Modification of the local environment to facilitate long-term colonisation is another possible function. Protection from acid is unlikely to be a primary role as the natural habitat of the organism St1 is the non-acid-secreting tissue of the small intestine.
Ferrero
R L
RL
School of Microbiology, University of New South Wales, Kensington, Australia.
Hazell
S L
SL
Lee
A
A
D000641:Ammonia / Q000494:pharmacology; D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D015153:Blotting, Western; D002167:Campylobacter / Q000201:enzymology*; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D005969:Glutamate Dehydrogenase / Q000032:analysis; D007082:Ileum / Q000382:microbiology; D012377:Rodentia; D014510:Urease / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification
D000641:Ammonia; D005969:Glutamate Dehydrogenase; D014510:Urease