Interaction Between Host Gastric Sialyl-Lewis X and H. pylori SabA Enhances H. pylori Density in Patients Lacking Gastric Lewis B Antigen

Sheu, Bor Shyang; Odenbreit, Stefan; Hung, Kuo Hsiang; Liu, Chia Pin; Sheu, Shew Meei; Yang, Hsiao Bai; Wu, Jiunn Jong

doi:10.1111/j.1572-0241.2006.00358.x

Cited by 85 publications

(103 citation statements)

References 14 publications

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“…The minimal structure required for SabA adhesin binding was shown to be NeuAcα2-3Gal (42,43). Accordingly, it has been demonstrated that SabA interaction with the host gastric sialyl-Le x antigen enhances H. pylori colonization in patients with weak or no Le b expression (44).…”

Section: Helicobacter Pylori Adhesion During Persistent Infectionmentioning

confidence: 99%

Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors

Magalhães

Reis

2010

Braz J Med Biol Res

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Section: Helicobacter Pylori Adhesion During Persistent Infectionmentioning

confidence: 99%

Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors

Magalhães

Reis

2010

Braz J Med Biol Res

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“…Boiled aliquots of bacterial lysates were subjected to sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, using a minigel apparatus (Bio-Rad), and blotted onto nitrocellulose membranes at 1 mA/cm 2 by use of a semidry blotting system (Biotec Fischer). The filters were blocked with 3% bovine serum albumin in Tris-buffered saline (TBS; 50 mM Tris-HCl, pH 7.5, 150 mM NaCl) and incubated with AK214 (AlpA) (36), AK262 (AlpB) (31), AK275 (BabC), AK276 (BabB), AK277 (BabA) (all described in reference 33), AK278 (SabA) (40), AK281 (HP0227) (this study), AK282 (OipA) (26), or AK257 (CagA) (34) antiserum for at least 4 hours. Either alkaline phosphatase-coupled protein A was used to visualize the antibody bound by decomposition of nitroblue tetrazolium or the blots were developed using horseradish peroxidase-coupled anti-rabbit immunoglobulin G and a Western Lightning detection system (Perkin-Elmer Life Sciences, Boston, MA).…”

Section: Methodsmentioning

confidence: 99%

Outer Membrane Protein Expression Profile in Helicobacter pylori Clinical Isolates

et al. 2009

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The gram-negative gastric pathogen Helicobacter pylori is equipped with an extraordinarily large set of outer membrane proteins (OMPs), whose role in the infection process is not well understood. The Hop (Helicobacter outer membrane porins) and Hor (Hop-related proteins) groups constitute a large paralogous family consisting of 33 members. The OMPs AlpA, AlpB, BabA, SabA, and HopZ have been identified as adhesins or adherenceassociated proteins. To better understand the relevance of these and other OMPs during infection, we analyzed the expression of eight different omp genes (alpA, alpB, babA, babB, babC, sabA, hopM, and oipA) in a set of 200 patient isolates, mostly from symptomatic children or young adults. Virtually all clinical isolates produced the AlpA and AlpB proteins, supporting their essential function. All other OMPs were produced at extremely variable rates, ranging from 35% to 73%, indicating a function in close adaptation to the individual host or gastric niche. In 11% of the isolates, BabA was produced, and SabA was produced in 5% of the isolates, but the strains failed to bind their cognate substrates. Interleukin-8 (IL-8) expression in gastric cells was strictly dependent on the presence of the cag pathogenicity island, whereas the presence of OipA clearly enhanced IL-8 production. The presence of the translocated effector protein CagA correlated well with BabA and OipA production. In conclusion, we found unexpectedly diverse omp expression profiles in individual H. pylori strains and hypothesize that this reflects the selective pressure for adhesion, which may differ across different hosts as well as within an individual over time.

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“…Adhesins with known ligands include SabA, BabA, and HpaA. SabA, a sialic acidbinding adhesin, functions as a hemagglutinin and has been associated with higher colonization density in humans (2,51). BabA binds the Lewis b blood group antigen (4).…”

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confidence: 99%

Helicobacter pylori AlpA and AlpB Bind Host Laminin and Influence Gastric Inflammation in Gerbils

et al. 2011

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Helicobacter pylori persistently colonizes humans, causing gastritis, ulcers, and gastric cancer. Adherence to the gastric epithelium has been shown to enhance inflammation, yet only a few H. pylori adhesins have been paired with targets in host tissue. The alpAB locus has been reported to encode adhesins involved in adherence to human gastric tissue. We report that abrogation of H. pylori AlpA and AlpB reduces binding of H. pylori to laminin while expression of plasmid-borne alpA or alpB confers laminin-binding ability to Escherichia coli. An H. pylori strain lacking only AlpB is also deficient in laminin binding. Thus, we conclude that both AlpA and AlpB contribute to H. pylori laminin binding. Contrary to expectations, the H. pylori SS1 mutant deficient in AlpA and AlpB causes more severe inflammation than the isogenic wild-type strain in gerbils. Identification of laminin as the target of AlpA and AlpB will facilitate future investigations of host-pathogen interactions occurring during H. pylori infection.

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Interaction Between Host Gastric Sialyl-Lewis X and H. pylori SabA Enhances H. pylori Density in Patients Lacking Gastric Lewis B Antigen

Abstract: In Taiwan, H. pylori isolates are 100% BabA-positive, but only 31% of them express SabA. The interaction between gastric sialyl-Le(x) and SabA of H. pylori determines the colonization density of patients expressing gastric Le(b) weakly or not at all.

Cited by 85 publications

References 14 publications

Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors

Helicobacter pylori adhesion to gastric epithelial cells is mediated by glycan receptors

Outer Membrane Protein Expression Profile in Helicobacter pylori Clinical Isolates

Helicobacter pylori AlpA and AlpB Bind Host Laminin and Influence Gastric Inflammation in Gerbils

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