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BabA-mediated adherence of pediatric ulcerogenic H-pylori strains to gastric mucins at neutral and acidic pH

Artikel i vetenskaplig tidskrift
Författare Macarena P Quintana-Hayashi
R. Rocha
Médea Padra
A. Thorell
Chunsheng Jin
Niclas G. Karlsson
M. Roxo-Rosa
M. Oleastro
Sara K. Lindén
Publicerad i Virulence
Volym 9
Nummer/häfte 1
Sidor 1699-1717
ISSN 2150-5594
Publiceringsår 2018
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 1699-1717
Språk en
Länkar dx.doi.org/10.1080/21505594.2018.15...
Ämnesord Mucin, Helicobacter pylori, peptic ulcer, adhesin, babA, children, binding, virulence, pH, glycosylation, antigen-binding adhesin, peptic-ulcer disease, c-terminal cleavage, gene-expression, clinical-relevance, dependent binding, mucosal barrier, infection, identification, glycoforms, Immunology, Infectious Diseases, Microbiology
Ämneskategorier Mikrobiologi inom det medicinska området

Sammanfattning

Helicobacter pylori infection can result in non-ulcer dyspepsia (NUD), peptic ulcer disease (PUD), adenocarcinoma, and gastric lymphoma. H. pylori reside within the gastric mucus layer, mainly composed of mucins carrying an array of glycan structures that can serve as bacterial adhesion epitopes. The aim of the present study was to characterize the binding ability, adhesion modes, and growth of H. pylori strains from pediatric patients with NUD and PUD to gastric mucins. Our results showed an increased adhesion capacity of pediatric PUD H. pylori strains to human and rhesus monkey gastric mucins compared to the NUD strains both at neutral and acidic pH, regardless if the mucins were positive for Lewis b (Le(b)), Sialyl-Lewis x (SLe(x)) or LacdiNAc. In addition to babA positive strains being more common among PUD associated strains, H. pylori babA positive strains bound more avidly to gastric mucins than NUD babA positive strains at acidic pH. Binding to Le(b) was higher among babA positive PUD H. pylori strains compared to NUD strains at neutral, but not acidic, pH. PUD derived babA-knockout mutants had attenuated binding to mucins and Le(b) at acidic and neutral pH, and to SLe(x) and DNA at acidic pH. The results highlight the role of BabA-mediated adherence of pediatric ulcerogenic H. pylori strains, and points to a role for BabA in adhesion to charged structures at acidic pH, separate from its specific blood group binding activity.

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