Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

Effects of pH on Helicobacter pylori binding to human gastric mucins: Identification of binding to non-MUC5AC mucins

In English

Författare

  • Sara Lindén
  • J Mahdavi
  • Jan Hedenbro
  • T Boren
  • Ingemar Carlstedt

Summary, in English

Helicobacter pylori causes gastritis, peptic ulcer disease and gastric cancer. The microbe is found in the gastric mucus layer where a pH gradient ranging from acidic in the lumen to neutral at the cell surface is maintained. The aim of the present study was to investigate the effects of pH on H. pylori binding to gastric mucins from healthy individuals. At pH 3, all strains bound to the most charged MUC5AC glycoform and to a putative mucin of higher charge and larger size than subunits of MUC5AC and MUC6, irrespective of host blood-group. In contrast, at pH 7.4 only Le(b)-binding BabA-positive strains bound to Le(b)-positive MUC5AC and to smaller mucin-like molecules, including MUC1. H. pylori binding to the latter component(s) seems to occur via the H-type-1 structure. All strains bound to a proteoglycan containing chondroitin sulphate/dermatan sulphate side chains at acidic pH, whereas binding to secreted MUC5AC and putative membrane-bound strains occurred both at neutral and acidic pH. The binding properties at acidic pH are thus common to all H. pylori strains, whereas mucin binding at neutral pH occurs via the bacterial BabA adhesin and the Le(b) antigen/related structures on the glycoprotein. Our work shows that microbe binding to membrane-bound mucins must be considered in H. pylori colonization, and the potential of these glycoproteins to participate in signalling events implies that microbe binding to such structures may initiate signal transduction over the epithelial layer. Competition between microbe binding to membrane-bound and secreted mucins is therefore an important aspect of host-microbe interaction.

Publiceringsår

2004

Språk

Engelska

Sidor

263-270

Publikation/Tidskrift/Serie

Biochemical Journal

Volym

384

Issue

2

Dokumenttyp

Artikel i tidskrift

Förlag

Portland Press

Ämne

  • Biochemistry and Molecular Biology

Nyckelord

  • mucosal protection
  • interaction
  • host-pathogen
  • Helicobacter pylori
  • gastric mucin
  • glycosylation
  • pH-depenclence

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0264-6021