The LacdiNAc-Specific Adhesin LabA Mediates Adhesion of Helicobacter pylori to Human Gastric Mucosa

• Type: Article in International Scientific Journal
• Date: 2014

Authors

Rossez, Y (Author) Other; Gosset, P (Author) Other; Boneca, IG (Author) Other; Magalhaes, A (Author) Other; Ecobichon, C (Author) Other; Celso Reis (Author) ICBAS; Cieniewski Bernard, C (Author) Other; Curt, MJC (Author) Other; Leonard, R (Author) Other; Maes, E (Author) Other; Sperandio, B (Author) Other; Slomianny, C (Author) Other; Sansonetti, PJ (Author) Other; Michalski, JC (Author) Other; Robbe Masselot, C (Author) Other

Journal

Title: Journal of Infectious Diseases

Vol. 210

Pages: 1286-1295

ISSN: 0022-1899

Publisher: Oxford University Press

Indexing

ISI Web of Knowledge - 68 Citations

Scopus - 71 Citations

Other information

Authenticus ID: P-009-ZP1

DOI: 10.1093/infdis/jiu239

Abstract (EN): Adhesion of Helicobacter pylori to the gastric mucosa is a necessary prerequisite for the pathogenesis of H. pylori-related diseases. In this study, we investigated the GalNAc beta 1-4GlcNAc motif (also known as N,N'-diacetyllactosediamine[ lacdiNAc]) carried by MUC5AC gastric mucins as the target for bacterial binding to the human gastric mucosa. The expression of LacdiNAc carried by gastric mucins was correlated with H. pylori localization, and all strains tested adhered significantly to this motif. Proteomic analysis and mutant construction allowed the identification of a yet uncharacterized bacterial adhesin, LabA, which specifically recognizes lacdiNAc. These findings unravel a target of adhesion for H. pylori in addition to moieties recognized by the well-characterized adhesins BabA and SabA. Localization of the LabA target, restricted to the gastric mucosa, suggests a plausible explanation for the tissue tropism of these bacteria. These results pave the way for the development of alternative strategies against H. pylori infection, using adherence inhibitors.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 10