Endoscopy 2004; 36 - 25
DOI: 10.1055/s-2004-825007

Helicobacter Pylori Interacts with the Human Single Domain Trefoil Protein, TFF1

M Clyne 1, P Dilon 1, S Daly 1, R O'Kennedy 1, F May 1, B Westley 1, B Drumm 1
  • 1The Childrens Research Centre, Our Lady's Hospital for Sick Children, Dublin 12, Ireland. The Conway Institute of Biomolecular and Biomedical Research, The Department of Paediatrics, University College Dublin and The Dublin Molecular Medicine Centre. The School of Biotechnology and The National Centre for Sensor Research, Dublin City University, Dublin 9. Department of Pathology, University of Newcastle upon Tyne, UK

Background & Aims: H. pylori is found in vivo in association with gastric mucus secreting cells, in the overlying gastric mucus but rarely if ever deep in gastric glands. This localization mirrors the expression of trefoil factor 1, TFF1. We tested the hypothesis that TFF1 is a receptor for H. pylori on the gastric mucosa possibly explaining why H. pylori only colonises the stomach.

Materials and Methods: Purified recombinant monomeric and dimeric human TFF1 were coated onto latex beads and binding of five H. pylori strains was assessed by flow cytometry. The BIAcore system based on the principle of surface plasmon resonance, which allows „real-time“ monitoring of molecular interactions at the sensor surface was used to further characterise the interaction of H. pylori with TFF1.

Results: All five strains bound to the TFF1 dimer, but not to the monomer or BSA. Binding was inhibited by a TFF1 monoclonal antibody and following preincubation of the bacteria with TFF1. E.coli HB101 and two C. jejuni isolates did not bind. Using the BIAcore system H. pylori bound strongly to TFF1-coated dextran chips (320RU) compared with uncoated chips (26RU). Preincubation of H. pylori with soluble TFF1 (1.56mg/ml) abolished binding. Preincubation of H. pylori with TFF1 enabled the organism to bind to porcine gastric mucin. Conclusions: TFF1 is a high affinity receptor for H. pylori which may explain the tropism of this organism for gastric tissue and the previously noted co-localisation of H. pylori with MUC5AC.