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

P. Parreira, A. Magalhães, C. A. Reis, T. Borén, Deborah E Leckband, M. C.L. Martins

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)8885-8893
Number of pages9
JournalActa Biomaterialia
Volume9
Issue number11
DOIs
StatePublished - Nov 1 2013

Fingerprint

Self assembled monolayers
Pathogens
Helicobacter pylori
Polysaccharides
Stomach
Antigens
Proteins
Adhesion
Bacterial Adhesins
Glycoproteins
Glycolipids
Scavenging
Biocompatible Materials
N-Acetylneuraminic Acid
Blood Group Antigens
Chelation
Biomaterials
Gold
Assays
Bacteria

Keywords

  • Blood group antigen binding adhesin
  • Functionalized nanostructured surfaces
  • Helicobacter pylori
  • Self-assembled monolayers
  • Sialic acid binding adhesin

ASJC Scopus subject areas

  • Biomaterials
  • Biomedical Engineering
  • Biotechnology
  • Biochemistry
  • Molecular Biology

Cite this

Bioengineered surfaces promote specific protein-glycan mediated binding of the gastric pathogen Helicobacter pylori. / Parreira, P.; Magalhães, A.; Reis, C. A.; Borén, T.; Leckband, Deborah E; Martins, M. C.L.

In: Acta Biomaterialia, Vol. 9, No. 11, 01.11.2013, p. 8885-8893.

Research output: Contribution to journalArticle

Parreira, P. ; Magalhães, A. ; Reis, C. A. ; Borén, T. ; Leckband, Deborah E ; Martins, M. C.L. / Bioengineered surfaces promote specific protein-glycan mediated binding of the gastric pathogen Helicobacter pylori. In: Acta Biomaterialia. 2013 ; Vol. 9, No. 11. pp. 8885-8893.
@article{0ee4173c97fc45e1aa19c4804bc592fd,
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 (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.",
keywords = "Blood group antigen binding adhesin, Functionalized nanostructured surfaces, Helicobacter pylori, Self-assembled monolayers, Sialic acid binding adhesin",
author = "P. Parreira and A. Magalh{\~a}es and Reis, {C. A.} and T. Bor{\'e}n and Leckband, {Deborah E} and Martins, {M. C.L.}",
year = "2013",
month = "11",
day = "1",
doi = "10.1016/j.actbio.2013.06.042",
language = "English (US)",
volume = "9",
pages = "8885--8893",
journal = "Acta Biomaterialia",
issn = "1742-7061",
publisher = "Elsevier BV",
number = "11",

}

TY - JOUR

T1 - Bioengineered surfaces promote specific protein-glycan mediated binding of the gastric pathogen Helicobacter pylori

AU - Parreira, P.

AU - Magalhães, A.

AU - Reis, C. A.

AU - Borén, T.

AU - Leckband, Deborah E

AU - Martins, M. C.L.

PY - 2013/11/1

Y1 - 2013/11/1

N2 - 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.

AB - 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.

KW - Blood group antigen binding adhesin

KW - Functionalized nanostructured surfaces

KW - Helicobacter pylori

KW - Self-assembled monolayers

KW - Sialic acid binding adhesin

UR - http://www.scopus.com/inward/record.url?scp=84885052038&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84885052038&partnerID=8YFLogxK

U2 - 10.1016/j.actbio.2013.06.042

DO - 10.1016/j.actbio.2013.06.042

M3 - Article

C2 - 23831721

AN - SCOPUS:84885052038

VL - 9

SP - 8885

EP - 8893

JO - Acta Biomaterialia

JF - Acta Biomaterialia

SN - 1742-7061

IS - 11

ER -