Isolation and characterisation of putative adhesins from Helicobacter pylori with affinity for heparan sulphate proteoglycan

Summary, in English

A pool of heparan sulphate-binding proteins (HSBPs) from Helicobacter pylori culture supernates was obtained by sequential ammonium sulphate precipitation and affinity chromatography on heparin-Sepharose, The chromatographic procedure yielded one major fraction that contained proteins with heparan sulphate affinity as revealed by inhibition studies of heparan sulphate binding to H. pylori cells. Preparative iso-electric focusing, SDS-PACE and blotting experiments, with peroxidase(POD)-labelled heparan sulphate as a probe, indicated the presence of two major extracellular proteins with POD-heparan sulphate affinity. One protein had a molecular mass of 66.2 kDa and a pI of 5.4, whilst the second protein had a molecular mass of 71.5 kDa and a pI of 5.0. The N-terminal amino acid sequence of the 71.5-kDa HSBP did not show homology to any other heparin-binding protein, nor to known proteins of H, pylori, whereas the 66.2-kDa HSBP showed a high homology to an Escherichia coli chaperon protein and equine haemoglobin. A third HSBP was isolated from an outer-membrane protein (OMP) fraction of H. pylori cells with a molecular mass of 47.2 kDa, The amino acid sequence of an internal peptide of the OMP-HSBP did not show homology to the extracellular HSBP of H, pylori, or to another microbial HSBP.

• Author: E. Ruiz-Bustos; J.L. Ochoa; Torkel Wadström; F. Ascencio
• Department/s: Division of Medical Microbiology
• Publishing year: 2001
• Language: English
• Pages: 215-222
• Publication/Series: Journal of Medical Microbiology
• Volume: 50
• Issue: 3
• Links: http://jmm.sgmjournals.org/cgi/content/abstract/50/3/215
• Document type: Journal article
• Publisher: Lippincott Williams & Wilkins
• Topic: Microbiology in the medical area
• Status: Published
• ISBN/ISSN/Other: ISSN: 0022-2615