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    Bioengineered surfaces promote specific protein–glycan mediated binding of the gastric pathogen Helicobacter pylori

    Year: 2013

    Journal: Acta Biomaterialia Volume 9, Issue 11, November 2013, Pages 8885–8893, 20131003

    Authors: P. Parreira 1 2, A. Magalhães 3, C.A. Reis 3 4 5, T. Borén 6, D. Leckband 7, M.C.L. Martins 1 5

    Last authors: M.C.L. Martins

    Organizations: 1 Instituto de Engenharia Biomédica (INEB), Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal 2 Faculdade de Engenharia, Universidade do Porto, Porto, Portugal 3 Instituto de Patologia e Imunologia Molecular da Universidade do Porto (IPATIMUP), Porto, Portugal 4 Faculdade de Medicina, Universidade do Porto, Porto, Portugal 5 Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, Porto, Portugal 6 Department of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå, Sweden 7 Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, IL, USA

    Country: USA, US, United States, United States of America, America, Sverige, Sweden, Portugal

    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 (Leb 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.