Isolation and characterisation of putative adhesins from Helicobacter pylori with affinity for heparan sulphate proteoglycan
(2001) In Journal of Medical Microbiology 50(3). p.215-222- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1119565
- author
- Ruiz-Bustos, E. ; Ochoa, J.L. ; Wadström, Torkel LU and Ascencio, F.
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Medical Microbiology
- volume
- 50
- issue
- 3
- pages
- 215 - 222
- publisher
- Lippincott Williams & Wilkins
- external identifiers
-
- wos:000167047100003
- scopus:0035113648
- ISSN
- 0022-2615
- language
- English
- LU publication?
- yes
- id
- 99a243fd-cc1e-477b-9666-f44509b99c62 (old id 1119565)
- alternative location
- http://jmm.sgmjournals.org/cgi/content/abstract/50/3/215
- date added to LUP
- 2016-04-01 17:15:35
- date last changed
- 2022-04-23 03:47:07
@article{99a243fd-cc1e-477b-9666-f44509b99c62,
abstract = {{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 = {{Ruiz-Bustos, E. and Ochoa, J.L. and Wadström, Torkel and Ascencio, F.}},
issn = {{0022-2615}},
language = {{eng}},
number = {{3}},
pages = {{215--222}},
publisher = {{Lippincott Williams & Wilkins}},
series = {{Journal of Medical Microbiology}},
title = {{Isolation and characterisation of putative adhesins from Helicobacter pylori with affinity for heparan sulphate proteoglycan}},
url = {{http://jmm.sgmjournals.org/cgi/content/abstract/50/3/215}},
volume = {{50}},
year = {{2001}},
}