Identification of heparan sulphate binding surface proteins of Helicobacter pylori: inhibition of heparan sulphate binding with sulphated carbohydrate polymers

Utt, Meeme; Wadström, Torkel

doi:10.1099/00222615-46-7-541

Cited by 43 publications

(34 citation statements)

References 26 publications

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“…Utt and Wadström (103) confirmed that binding of heparan sulfate by H. pylori at pH 4 to 6 is very common among H. pylori strains. As the previous study had indicated, inhibitory assays with various compounds such as dextran sulfate and carrageenans revealed that inhibition was related to the sulfate content of the molecule, not to the carbohydrate polymer backbone.…”

Section: Heparin and Heparan Sulfatementioning

confidence: 52%

Helicobacter pylori Interactions with Host Serum and Extracellular Matrix Proteins: Potential Role in the Infectious Process

Dubreuil¹,

Giudice²,

Rappuoli³

2002

Microbiol Mol Biol Rev

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Helicobacter pylori, a gram-negative spiral-shaped bacterium, specifically colonizes the stomachs of humans. Once established in this harsh ecological niche, it remains there virtually for the entire life of the host. To date, numerous virulence factors responsible for gastric colonization, survival, and tissue damage have been described for this bacterium. Nevertheless, a critical feature of H. pylori is its ability to establish a long-lasting infection. In fact, although good humoral (against many bacterial proteins) and cellular responses are observed, most infected persons are unable to eradicate the infection. A large body of evidence has shown that the interaction between H. pylori and the host is very complex. In addition to the effect of virulence factors on colonization and persistence, binding of specialized bacterial proteins, known as receptins, to certain host molecules (ligands) could explain the success of H. pylori as a chronically persisting pathogen. Some of the reported interactions are of high affinity, as revealed by their calculated dissociation constant. This review examines the binding of host proteins (serum and extracellular matrix proteins) to H. pylori and considers the significance of these interactions in the infectious process. A more thorough understanding of the kinetics of these receptin interactions could provide a new approach to preventing deeper tissue invasion in H. pylori infections and could represent an alternative to antibiotic treatment

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Section: Heparin and Heparan Sulfatementioning

confidence: 52%

Helicobacter pylori Interactions with Host Serum and Extracellular Matrix Proteins: Potential Role in the Infectious Process

Dubreuil¹,

Giudice²,

Rappuoli³

2002

Microbiol Mol Biol Rev

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“…Studies have shown the presence of HSBP in H. pylori [18,19,28,45], where the interaction of these bacterial proteins with host components was exploited. It could be determined that these proteins recognised heparin, gastrointestinal cell surface HS, in an association inhibitable by the presence of sulphated carbohydrate polymers in the media.…”

Section: Discussionmentioning

confidence: 99%

“…pylori strain 25 (clinical isloate from adenocarcinoma) was provided by Professor T. Wadstro Èm (Lund University, Sweden). This strain, which has previously been examined for haemagglutinins [18] and was also found to bind HS with high af®nity [28], was selected for characterisation of HSBPs.…”

Section: Bacterial Strain and Growth Conditionsmentioning

confidence: 99%

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

Ruíz-Bustos¹,

Ochoa²,

Wadström

et al. 2001

Journal of Medical Microbiology

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A pool of heparan sulphate-binding proteins (HSBPs) from Helicobacter pylori culture supernates was obtained by sequential ammonium sulphate precipitation and af®nity chromatography on heparin-Sepharose. The chromatographic procedure yielded one major fraction that contained proteins with heparan sulphate af®nity as revealed by inhibition studies of heparan sulphate binding to H. pylori cells. Preparative iso-electric focusing, SDS-PAGE and blotting experiments, with peroxidase(POD)-labelled heparan sulphate as a probe, indicated the presence of two major extracellular proteins with POD-heparan sulphate af®nity. 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.

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“…A heparin-binding protein was located at the cell surface by biotinylation and indirect immunofluorescence assays. This protein corresponded to a 55-60 kDa molecule (Utt & Wadstrom, 1997 terial recruitment of molecules, such as heparin, in the immediate environment during the infectious process. These molecules can then serve as universal binding sites for various mammalian heparin-binding proteins.…”

Section: Introductionmentioning

confidence: 99%

Effect of heparin binding on Helicobacter pylori resistance to serum

Dubreuil

Ruggiero

Rappuoli

et al. 2004

Journal of Medical Microbiology

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Identification of heparan sulphate binding surface proteins of Helicobacter pylori: inhibition of heparan sulphate binding with sulphated carbohydrate polymers

Abstract: Heparan sulphate binding to cells of the gastric pathogen

Cited by 43 publications

References 26 publications

Helicobacter pylori Interactions with Host Serum and Extracellular Matrix Proteins: Potential Role in the Infectious Process

Helicobacter pylori Interactions with Host Serum and Extracellular Matrix Proteins: Potential Role in the Infectious Process

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

Effect of heparin binding on Helicobacter pylori resistance to serum

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