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Bioengineered surfaces promote specific protein-glycan mediated binding of the gastric pathogen Helicobacter pylori(Article)
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- aInstituto de Engenharia Biomédica (INEB), Universidade Do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal
- bFaculdade de Engenharia, Universidade Do Porto, Porto, Portugal
- cInstituto de Patologia e Imunologia Molecular da Universidade Do Porto (IPATIMUP), Porto, Portugal
- dFaculdade de Medicina, Universidade Do Porto, Porto, Portugal
- eInstituto de Ciências Biomédicas Abel Salazar, Universidade Do Porto, Porto, Portugal
- fDepartment of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden
- gDepartment of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, IL, United States
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Abstract
Helicobacter pylori colonizes the gastric mucosa of half of the worlds population and persistent infection is related with an increase in the risk of gastric cancer. Adhesion of H. pylori to the gastric epithelium, which is essential for infection, is mediated by bacterial adhesin proteins that recognize specific glycan structures (Gly-R) expressed in the gastric mucosa. The blood group antigen binding adhesin (BabA) recognizes difucosylated antigens such as Lewis B (Leb), while the sialic acid binding adhesin (SabA) recognizes sialylated glycoproteins and glycolipids, such as sialyl-Lewis x (sLex). This work aimed to investigate whether these Gly-Rs (Le b and sLex) can attract and specifically bind H. pylori after immobilization on synthetic surfaces (self-assembled monolayers (SAMs) of alkanethiols on gold). Functional bacterial adhesion assays for (Gly-R)-SAMs were performed using H. pylori strains with different adhesin protein profiles. The results demonstrate that H. pylori binding to surfaces occurs via interaction between its adhesins and cognate (Gly-R)-SAMs and bound H. pylori maintains its characteristic rod-shaped morphology only during conditions of specific adhesin-glycan binding. These results offer new insights into innovative strategies against H. pylori infection based on the scavenging of bacteria from the stomach using specific H. pylori chelating biomaterials. © 2013 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.
Indexed keywords
| EMTREE drug terms: | adhesinblood group antigenglycanlewis b antigenself assembled monolayersialoglycoproteinsialyl Lewis x antigenunclassified drug |
|---|---|
| EMTREE medical terms: | articlebacterial strainbacterium adherencebinding affinitybioengineeringblood group Lewis systemcontrolled studyHelicobacter pyloriimmobilizationnonhumanpriority journalprotein bindingsurface property |
| Species Index: | Bacteria (microorganisms)Helicobacter pylori |
| Medline keywords: | Blood group antigen binding adhesinFunctionalized nanostructured surfacesHelicobacter pyloriSelf-assembled monolayersSialic acid binding adhesin |
| MeSH: | Adhesins, BacterialAdsorptionAvidinBacterial AdhesionBioengineeringBiotinGlycosphingolipidsHelicobacter pyloriImmobilized ProteinsKineticsPolysaccharidesQuartz Crystal Microbalance TechniquesStomachSurface Properties |
Funding details
| Funding sponsor | Funding number | Acronym |
|---|---|---|
| Programa Operacional Temático Factores de Competitividade | COMPETE | |
| SFRH/BD/39931/2007,NSF DMR 08735,SFRH/BPD/75871/2011 | ||
| Vetenskapsrådet | 11218 | |
| Fundação para a Ciência e a Tecnologia See opportunities | PTDC/CTM/65330/2006,PTDC/CTM-BPC/121149/2010,FCOMP-01-0124-FEDER-020073,PEst-C/SAU/LA0002/2011 | |
| Fundação para a Ciência e a Tecnologia See opportunities |
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1
This work was financed by FEDER funds through the Programa Operacional Factores de Competitividade (COMPETE) and by Portuguese funds through the Fundação para a Ciência e a Tecnologia (FCT) within the framework of the projects PTDC/CTM/65330/2006 , PTDC/CTM-BPC/121149/2010 , FCOMP-01-0124-FEDER-020073 and PEst-C/SAU/LA0002/2011 and by Grants to T.B. from the Swedish Research Council (Grant no. 11218 ), the Swedish Cancer Foundations , and the J.C. Kempe and Seth M. Kempe Memorial Foundation . The authors would like to thank the Max-Planck Institut für Infektionsbiology, Berlin, Germany, for providing the H. pylori strains. P.P. and A.M. acknowledge the FCT for PhD Grant SFRH/BD/39931/2007 and post-doctoral fellowship SFRH/BPD/75871/2011 , respectively. D.E.L. is supported by Grant NSF DMR 08735. The authors thank Maria Gómez Lázaro, of the Bioimaging Center for Biomaterials and Regenerative Therapies (b.IMAGE) of the Instituto de Engenharia Biomédica, Universidade do Porto, for help with the confocal microscopy.
- ISSN: 17427061
- Source Type: Journal
- Original language: English
- DOI: 10.1016/j.actbio.2013.06.042
- PubMed ID: 23831721
- Document Type: Article
Martins, M.C.L.; Instituto de Engenharia Biomédica (INEB), Universidade Do Porto, Rua do Campo Alegre 823, Portugal;
© Copyright 2013 Elsevier B.V., All rights reserved.
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