pH-dependent binding of Helicobacter pylori to pig gastric mucins

Citation
H. Nordman et al., pH-dependent binding of Helicobacter pylori to pig gastric mucins, FEMS IM MED, 24(2), 1999, pp. 175-181
Citations number
18
Categorie Soggetti
Immunology
Journal title
FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY
ISSN journal
09288244 → ACNP
Volume
24
Issue
2
Year of publication
1999
Pages
175 - 181
Database
ISI
SICI code
0928-8244(199906)24:2<175:PBOHPT>2.0.ZU;2-B
Abstract
A microtiter-based assay was developed to study the binding of Helicobacter pylori to pig gastric mucins purified by density-gradient centrifugation i n CsCl/4 M guanidinium chloride. Binding of H. pylori was observed over the 'mucin' band as well as with 'low-density' components in the gradients, an d binding to the latter was more pronounced when incubations were performed at 37 degrees C as compared to 20 degrees C. At a lower pH, binding of H. pylori (strain SVA 40) to the 'high-density' mucins from pig antrum was inc reased but binding to the 'low-density' ones was decreased. Binding of the P466 strain (Le(b)-specific) was mainly associated with the 'mucin' band, w hereas the MO19 strain reacted preferentially with the 'low-density' compon ents. In summary, H. pylori may bind to gastric mucins and the binding is i nfluenced by temperature, pH and the repertoire of bacterial adhesins. (C) 1999 Federation of European Microbiological Societies. Published by Elsevie r Science B.V. All rights reserved.