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

• Tipo: Artigo em Revista Científica Internacional
• Data: 2014

Autores

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

Revista

Título: Journal of Infectious Diseases

Vol. 210

Páginas: 1286-1295

ISSN: 0022-1899

Editora: Oxford University Press

Indexação

ISI Web of Knowledge - 68 Citações

Scopus - 71 Citações

Outras Informações

ID Authenticus: 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 10