To the top

Page Manager: Webmaster
Last update: 9/11/2012 3:13 PM

Tell a friend about this page
Print version

SabA is the H. pylori hem… - University of Gothenburg, Sweden Till startsida
Sitemap
To content Read more about how we use cookies on gu.se

SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans.

Journal article
Authors Marina Aspholm
Farzad O Olfat
Jenny Nordén
Berit Sondén
Carina Lundberg
Rolf Sjöström
Siiri Altraja
Stefan Odenbreit
Rainer Haas
Torkel Wadström
Lars Engstrand
Cristina Semino-Mora
Hui Liu
André Dubois
Susann Teneberg
Anna Arnqvist
Thomas Borén
Published in PLoS pathogens
Volume 2
Issue 10
Pages e110
ISSN 1553-7374
Publication year 2006
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages e110
Language en
Links dx.doi.org/10.1371/journal.ppat.002...
Keywords Adhesins, Bacterial, genetics, metabolism, Adsorption, Animals, Antigens, Bacterial, metabolism, Bacterial Adhesion, Binding Sites, Binding, Competitive, Capillaries, Erythrocytes, metabolism, microbiology, Gangliosides, metabolism, Gastric Mucosa, blood supply, microbiology, Gene Deletion, Helicobacter Infections, immunology, microbiology, Helicobacter pylori, metabolism, physiology, Hemagglutination, Hemagglutinins, metabolism, Humans, Macaca mulatta, N-Acetylneuraminic Acid, metabolism, Oligosaccharides, metabolism, Polysaccharides, metabolism, Venules
Subject categories Medical and Health Sciences

Abstract

Adherence of Helicobacter pylori to inflamed gastric mucosa is dependent on the sialic acid-binding adhesin (SabA) and cognate sialylated/fucosylated glycans on the host cell surface. By in situ hybridization, H. pylori bacteria were observed in close association with erythrocytes in capillaries and post-capillary venules of the lamina propria of gastric mucosa in both infected humans and Rhesus monkeys. In vivo adherence of H. pylori to erythrocytes may require molecular mechanisms similar to the sialic acid-dependent in vitro agglutination of erythrocytes (i.e., sialic acid-dependent hemagglutination). In this context, the SabA adhesin was identified as the sialic acid-dependent hemagglutinin based on sialidase-sensitive hemagglutination, binding assays with sialylated glycoconjugates, and analysis of a series of isogenic sabA deletion mutants. The topographic presentation of binding sites for SabA on the erythrocyte membrane was mapped to gangliosides with extended core chains. However, receptor mapping revealed that the NeuAcalpha2-3Gal-disaccharide constitutes the minimal sialylated binding epitope required for SabA binding. Furthermore, clinical isolates demonstrated polymorphism in sialyl binding and complementation analysis of sabA mutants demonstrated that polymorphism in sialyl binding is an inherent property of the SabA protein itself. Gastric inflammation is associated with periodic changes in the composition of mucosal sialylation patterns. We suggest that dynamic adaptation in sialyl-binding properties during persistent infection specializes H. pylori both for individual variation in mucosal glycosylation and tropism for local areas of inflamed and/or dysplastic tissue.

Page Manager: Webmaster|Last update: 9/11/2012
Share:

The University of Gothenburg uses cookies to provide you with the best possible user experience. By continuing on this website, you approve of our use of cookies.  What are cookies?