Structure, function and localization of Helicobacter pylori urease. Yale J Biol Med 1998;71(2):63-73
Date
06/23/1999Pubmed ID
10378351Pubmed Central ID
PMC2578883Scopus ID
2-s2.0-0032450789 (requires institutional sign-in at Scopus site) 51 CitationsAbstract
Helicobacter pylori is the causative agent of most cases of gastritis. Once acquired, H. pylori establishes chronic persistent infection; it is this long-term infection that, is a subset of patients, leads to gastric or duodenal ulcer, gastric cancer or gastric MALT lymphoma. All fresh isolates of H. pylori express significant urease activity, which is essential to survival and pathogenesis of the bacterium. A significant fraction of urease is associated with the surface of H. pylori both in vivo and in vitro. Surface-associated urease is essential for H. pylori to resist exposure to acid in the presence of urea. The mechanism whereby urease becomes associated with the surface of H. pylori is unique. This process, which we term "altruistic autolysis," involves release of urease (and other cytoplasmic proteins) by genetically programmed autolysis with subsequent adsorption of the released urease onto the surface of neighboring intact bacteria. To our knowledge, this is the first evidence of essential communal behavior in pathogenic bacteria; such behavior is crucial to understanding the pathogenesis of H. pylori.
Author List
Dunn BE, Phadnis SHMESH terms used to index this publication - Major topics in bold
Bacterial ProteinsCell Membrane
Heat-Shock Proteins
Helicobacter Infections
Helicobacter pylori
Humans
Subcellular Fractions
Urease
Vaccines
