Type

Journal Article

Authors

Marguerite Clyne
Brendan Drumm
Angeline Smith
Sebastian Suerbaum
Melanie Rust
Christine Josenhans
Bruce R Westley
Felicity E B May
Richard O'Kennedy
Stephen Hearty
and 3 others

Subjects

Microbiology

Topics
tumor suppressor proteins bacterial adhesion helicobacter pylori hydrogen ion concentration pathology humans metabolism physiology flow cytometry gastric mucosa child isolation purification electrophoresis polyacrylamide gel helicobacter infections colony count microbial lipopolysaccharides tff1 protein human microbiology lipopolysaccharide helicobacter pylori

Helicobacter pylori lipopolysaccharide interacts with TFF1 in a pH-dependent manner. (2008)

Abstract Little is known about how bacteria establish chronic infections of mucosal surfaces. Helicobacter pylori (H. pylori), a chronic pathogen that lives in the gastric mucosa of humans, interacts with the trefoil factor family (TFF) protein TFF1, which is found in gastric mucus. We aimed to characterize the interaction of H. pylori with TFF1 and to assess the role of this interaction in mediating colonization. Subcellular fractions of H. pylori were immobilized and then probed with TFF1, TFF2, or TFF3. The effect of glycosidases and preincubation with monosaccharides on the interaction and binding of TFF1 to a H. pylori adhesin was assessed. The interaction between H. pylori adhesin and TFF1 was characterized using surface plasmon resonance, flow cytometry, nondenaturing polyacrylamide gel electrophoresis, coimmunofluoresence, and incubation with tissue sections. The H. pylori core oligosaccharide portion (rough form) of lipopolysaccharide (RF-LPS) bound to TFF1 and to a lesser extent TFF3; this interaction was inhibited by incubation of RF-LPS with mannosidase, glucosidase, or mixed monosaccharides. TFF1 also bound to human serum albumin-conjugated mannose and glucose. The optimum pH for binding was 5.0-6.0 for TFF1 and 7.0 for TFF3. H. pylori bound TFF1 in gastric mucus ex vivo; binding of LPS-coated latex beads to human antral gastric tissue was inhibited by TFF1. TFF1 interacts specifically with H. pylori RF-LPS. The pH dependence of this interaction indicates that binding of H. pylori to TFF1 in the stomach could promote colonization of the mucus layer adjacent to the gastric epithelial surface.
Collections Ireland -> University College Dublin -> PubMed

Full list of authors on original publication

Marguerite Clyne, Brendan Drumm, Angeline Smith, Sebastian Suerbaum, Melanie Rust, Christine Josenhans, Bruce R Westley, Felicity E B May, Richard O'Kennedy, Stephen Hearty and 3 others

Experts in our system

1
Marguerite Clyne
University College Dublin
Total Publications: 36
 
2
B Drumm
University College Dublin
Total Publications: 38
 
3
R O'Kennedy
Dublin City University
Total Publications: 197
 
4
Stephen Hearty
Dublin City University
Total Publications: 27