title: Biochemical aspects of H. pylori adhesion.
abstract: In analogy with Vibrio cholerae and other toxigenic enteropathogens such as Yersinia enterocolitica it seems most likely today that H. pylori by specific surface proteins binds to epithelial cell receptors (Table 1) allowing the pathogen to deliver urease, vacuolating toxin and other toxic metabolites to cause tissue damage and inflammation (1-3). H. pylori as well as animal gastric pathogens as H. mustelae and H. felis have developed an efficient flagellar apparatus allowing rapid and efficient penetration of the gastric mucus layer (3). Most interestingly, flagellae seems to be synthesized in the late stage of growth before the switch of spiral-shaped organisms to coccoidal forms in a liquid medium.
authors.affiliation: Department of Medical Microbiology, Lund University, Sweden.
authors.forename: T
authors.initials: T
authors.lastname: Wadström
authors.forename: S
authors.initials: S
authors.lastname: Hirmo
authors.forename: B
authors.initials: B
authors.lastname: Nilsson
mesh_terms: D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D015374:Biosensing Techniques; D005753:Gastric Mucosa / Q000378:metabolism / Q000382:microbiology; D006017:Glycolipids / Q000378:metabolism; D016480:Helicobacter pylori / Q000378:metabolism*; D006801:Humans; D037102:Lectins / Q000502:physiology; D009093:Mucus / Q000378:metabolism / Q000382:microbiology; D010743:Phospholipids / Q000378:metabolism; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D006017:Glycolipids; D037102:Lectins; D010743:Phospholipids; D011956:Receptors, Cell Surface