The MUC5AC Glycoprotein is the Primary Receptor for <i>Helicobacter pylori</i> in the Human Stomach

Bovenkamp, Jeroen H.B. Van de; Mahdavi, Jafar; Male, Anita M. Korteland-van; Büller, Hans A.; Einerhand, Alexandra W. C.; Borén, Thomas; Dekker, Jan

doi:10.1046/j.1523-5378.2003.00173.x

Cited by 124 publications

(119 citation statements)

References 50 publications

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“…However, only strains of H. pylori that express the BabA adhesin are capable of binding to Le b (33). Furthermore, H. pylori can bind to MUC5AC in the absence of Le b (11). In our study, there was no correlation between the ability of the H. pylori strains to bind Le b and to bind TFF1, as all strains bound to TFF1 and only one bound to Le b .…”

Section: Discussioncontrasting

confidence: 65%

“…However, other adhesins such as the AlpA and AlpB proteins have been identified, but no receptor for these proteins has been identified (10), indicating that other receptors exist on the gastric mucosa. In addition, neither Le b nor Le x is expressed solely in the stomach, and H. pylori also binds in vitro to Le b expressed on duodenal tissue (11), which is never observed in vivo. In contrast, areas of gastric metaplasia in the duodenum can be colonized in vivo, indicating that there is a receptor for H. pylori specific for gastric tissue.…”

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confidence: 96%

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Helicobacter pylori interacts with the human single-domain trefoil protein TFF1

Clyne

Dillon

Daly

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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Why Helicobacter pylori colonizes only gastric tissue is unknown. It is found on gastric mucus-secreting cells and in the overlying gastric mucus but not deep in gastric glands. This localization mirrors the expression of trefoil factor 1, TFF1. We hypothesized that H. pylori interacting with TFF1 could explain the tropism of this bacteria for gastric tissue. Recombinant human TFF1 expressed in Escherichia coli was purified by affinity chromatography, ionexchange chromatography, and gel filtration. Binding of H. pylori was assessed by using flow cytometry and the BIAcore system, which allows real-time monitoring of molecular interactions. In flow cytometry, H. pylori bound to the TFF1 dimer, but Campylobacter jejuni strains and the laboratory strain of E. coli, HB101, did not bind. When the BIAcore system was used, H. pylori bound strongly to TFF1-coated dextran chips compared with uncoated chips. Binding was inhibited by a TFF1 monoclonal antibody and by soluble TFF1. H. pylori bound to porcine gastric mucin only if it was pretreated with TFF1. In conclusion, H. pylori interacts avidly with the dimeric form of TFF1, and this interaction enables binding to gastric mucin, suggesting that TFF1 may act as a receptor for the organism in vivo. This interaction may underline the previously unexplained tropism of this organism for gastric tissue and its colocalization with the gastric mucin MUC5AC.

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Section: Discussioncontrasting

confidence: 65%

mentioning

confidence: 96%

Helicobacter pylori interacts with the human single-domain trefoil protein TFF1

Clyne

Dillon

Daly

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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“…Red fluorochromes such as TRITC or Texas-Red can be used equivalently ( Van de Bovenkamp et al, 2003), although TRITC tends to leach from bacterial cells and skew adherence profiles unless tissue sections are very thoroughly washed after the bacterial overlay. It is also important to take into consideration that bacterial surface labeling involves modification of basic amino acids and thus may diminish adherence by direct inactivation of an adhesin's binding domain or indirectly through steric hindrance.…”

Section: Characterization Of Bacterial Adherence By In Vitro Binding mentioning

confidence: 99%

Helicobacter pylori Adhesion to Carbohydrates

Aspholm¹,

Kalia²,

Rühl³

et al. 2006

Methods in Enzymology

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Adherence of bacterial pathogens to host tissues contributes to colonization and virulence and typically involves specific interactions between bacterial proteins called adhesins and cognate oligosaccharide (glycan) or protein motifs in the host that are used as receptors. A given pathogen may have multiple adhesins, each specific for a different set of receptors and, potentially, with different roles in infection and disease. This chapter provides strategies for identifying and analyzing host glycan receptors and the bacterial adhesins that exploit them as receptors, with particular reference to adherence of the gastric pathogen Helicobacter pylori.

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“…Normal gastric mucosa shows cell type specific expression of secreted mucin MUC5AC in the surface epithelium (Wang et al, 2006;Lindén et al, 2010). Several studies have strongly suggested that MUC5AC forms the major receptor for H. pylori in the human stomach (Van de Bovenkamp et al, 2003;Lindén et al, 2008), and the infection of H. pylori can alter the expression of MUC5AC (Kocer et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Common Genetic Variations in the MUC5AC Gene are Not Related to Helicobacter pylori Serologic Status

Zhou

Zhang²,

Gao³

et al. 2015

Asian Pacific Journal of Cancer Prevention

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Several lines of evidence suggest that MUC5AC genetic polymorphisms might confer susceptibility to H. pylori infection and therefore gastric cancer risk. We here assessed the association of common polymorphisms in the MUC5AC gene with H. pylori seroprevalence using an LD-based tagSNP approach in a north-western Chinese Han population. A total of 12 tagSNPs were successfully genotyped among 281 unrelated ethnic Han Chinese who had no cancer history, and no identifiable gastric disease or genetic disease. No significant association between any alleles, genotypes or haplotypes and H. pylori seroprevalence was observed. Our results suggest that common genetic variations in MUC5AC gene might not make a major contribution to the risk of H. pylori infection.

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The MUC5AC Glycoprotein is the Primary Receptor for Helicobacter pylori in the Human Stomach

Abstract: Mucin MUC5AC is the most important carrier of the LeB carbohydrate structure in normal gastric tissue and forms the major receptor for H. pylori.

Cited by 124 publications

References 50 publications

Helicobacter pylori interacts with the human single-domain trefoil protein TFF1

Helicobacter pylori interacts with the human single-domain trefoil protein TFF1

Helicobacter pylori Adhesion to Carbohydrates

Common Genetic Variations in the MUC5AC Gene are Not Related to Helicobacter pylori Serologic Status

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