title: Bioengineered surfaces promote specific protein-glycan mediated binding of the gastric pathogen Helicobacter pylori.
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 (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.
authors.affiliation: Instituto de Engenharia Biomédica (INEB), Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; Faculdade de Engenharia, Universidade do Porto, Porto, Portugal.
authors.forename: P
authors.initials: P
authors.lastname: Parreira
authors.forename: A
authors.initials: A
authors.lastname: Magalhães
authors.forename: C A
authors.initials: CA
authors.lastname: Reis
authors.forename: T
authors.initials: T
authors.lastname: Borén
authors.forename: D
authors.initials: D
authors.lastname: Leckband
authors.forename: M C L
authors.initials: MC
authors.lastname: Martins
mesh_terms: D018829:Adhesins, Bacterial / Q000378:metabolism*; D000327:Adsorption; D001360:Avidin / Q000378:metabolism; D001422:Bacterial Adhesion; D057005:Bioengineering; D001710:Biotin / Q000378:metabolism; D006028:Glycosphingolipids / Q000378:metabolism; D016480:Helicobacter pylori / Q000166:cytology / Q000502:physiology*; D055767:Immobilized Proteins / Q000378:metabolism; D007700:Kinetics; D011134:Polysaccharides / Q000378:metabolism*; D058525:Quartz Crystal Microbalance Techniques; D013270:Stomach / Q000382:microbiology*; D013499:Surface Properties
chemical_list: D018829:Adhesins, Bacterial; D006028:Glycosphingolipids; D055767:Immobilized Proteins; D011134:Polysaccharides; C093483:neutravidin; D001360:Avidin; D001710:Biotin
keywords: Blood group antigen binding adhesin; Functionalized nanostructured surfaces; Helicobacter pylori; Self-assembled monolayers; Sialic acid binding adhesin