title: Escherichia coli common pilus (ECP) targets arabinosyl residues in plant cell walls to mediate adhesion to fresh produce plants.
abstract: Outbreaks of verotoxigenic Escherichia coli are often associated with fresh produce. However, the molecular basis to adherence is unknown beyond ionic lipid-flagellum interactions in plant cell membranes. We demonstrate that arabinans present in different constituents of plant cell walls are targeted for adherence by E. coli common pilus (ECP; or meningitis-associated and temperature-regulated (Mat) fimbriae) for E. coli serotypes O157:H7 and O18:K1:H7. l-Arabinose is a common constituent of plant cell wall that is rarely found in other organisms, whereas ECP is widespread in E. coli and other environmental enteric species. ECP bound to oligosaccharides of at least arabinotriose or longer in a glycan array, plant cell wall pectic polysaccharides, and plant glycoproteins. Recognition overlapped with the antibody LM13, which binds arabinanase-sensitive pectic epitopes, and showed a preferential affinity for (1→5)-α-linked l-arabinosyl residues and longer chains of arabinan as demonstrated with the use of arabinan-degrading enzymes. Functional adherence in planta was mediated by the adhesin EcpD in combination with the structural subunit, EcpA, and expression was demonstrated with an ecpR-GFP fusion and ECP antibodies. Spinach was found to be enriched for ECP/LM13 targets compared with lettuce. Specific recognition of arabinosyl residues may help explain the persistence of E. coli in the wider environment and association of verotoxigenic E. coli with some fresh produce plants by exploitation of a glycan found only in plant, not animal, cells.
authors.affiliation: From the Cellular and Molecular Sciences, James Hutton Institute, Dundee DD2 5DA, Scotland, United Kingdom and.
authors.forename: Yannick
authors.initials: Y
authors.lastname: Rossez
authors.affiliation: From the Cellular and Molecular Sciences, James Hutton Institute, Dundee DD2 5DA, Scotland, United Kingdom and.
authors.forename: Ashleigh
authors.initials: A
authors.lastname: Holmes
authors.affiliation: Department of Plant Biology and Biotechnology, University of Copenhagen, 1871 Frederiksberg Copenhagen, Denmark.
authors.forename: Henriette
authors.initials: H
authors.lastname: Lodberg-Pedersen
authors.affiliation: From the Cellular and Molecular Sciences, James Hutton Institute, Dundee DD2 5DA, Scotland, United Kingdom and.
authors.forename: Louise
authors.initials: L
authors.lastname: Birse
authors.affiliation: From the Cellular and Molecular Sciences, James Hutton Institute, Dundee DD2 5DA, Scotland, United Kingdom and.
authors.forename: Jacqueline
authors.initials: J
authors.lastname: Marshall
authors.affiliation: Department of Plant Biology and Biotechnology, University of Copenhagen, 1871 Frederiksberg Copenhagen, Denmark.
authors.forename: William G T
authors.initials: WG
authors.lastname: Willats
authors.affiliation: From the Cellular and Molecular Sciences, James Hutton Institute, Dundee DD2 5DA, Scotland, United Kingdom and.
authors.forename: Ian K
authors.initials: IK
authors.lastname: Toth
authors.affiliation: From the Cellular and Molecular Sciences, James Hutton Institute, Dundee DD2 5DA, Scotland, United Kingdom and nicola.holden@hutton.ac.uk.
authors.forename: Nicola J
authors.initials: NJ
authors.lastname: Holden
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D000911:Antibodies, Monoclonal / Q000737:chemistry; D000918:Antibody Specificity; D001089:Arabinose / Q000737:chemistry* / Q000378:metabolism; D001422:Bacterial Adhesion; D002473:Cell Wall / Q000737:chemistry* / Q000378:metabolism / Q000382:microbiology; D019453:Escherichia coli O157 / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D036781:Fimbriae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010861:Fimbriae, Bacterial / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D054884:Host-Pathogen Interactions; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D059828:Plant Cells / Q000737:chemistry / Q000378:metabolism / Q000382:microbiology; D011134:Polysaccharides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D018724:Spinacia oleracea / Q000737:chemistry / Q000378:metabolism / Q000382:microbiology
chemical_list: D018829:Adhesins, Bacterial; D000911:Antibodies, Monoclonal; C571837:EcpA protein, E coli; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D011134:Polysaccharides; D011994:Recombinant Proteins; C082574:ecpD protein, E coli; C030080:araban; D036781:Fimbriae Proteins; D001089:Arabinose
keywords: Adhesin; Arabinose; Bacterial Adhesion; Escherichia coli (E. coli); Glycan Array; Glycobiology; Host-Pathogen Interaction; Ligand-binding Protein; Organelle; Plant Cell Wall