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Lookup NU author(s): Professor William WillatsORCiD
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).
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.
Author(s): Rossez Y, Holmes A, Lodberg-Pedersen H, Birse L, Marshall J, Willats WGT, Toth IK, Holden NJ
Publication type: Article
Publication status: Published
Journal: The Journal of Biological Chemistry
Year: 2014
Volume: 289
Issue: 49
Pages: 34349-34365
Print publication date: 05/12/2014
Online publication date: 15/10/2014
Acceptance date: 01/01/1900
Date deposited: 17/02/2017
ISSN (electronic): 1083-351X
URL: http://dx.doi.org/10.1074/jbc.M114.587717
DOI: 10.1074/jbc.M114.587717
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