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ORIGINAL RESEARCH article

Front. Microbiol.
Sec. Microbial Physiology and Metabolism
Volume 16 - 2025 | doi: 10.3389/fmicb.2025.1507286

Biochemical characterization of the Escherichia coli surfaceome: A focus on type I fimbriae and flagella

Provisionally accepted
Devon William Kavanaugh Devon William Kavanaugh 1*Adeline SIVIGNON Adeline SIVIGNON 1Yannick Rossez Yannick Rossez 2Zina Chouit Zina Chouit 2Christophe Chambon Christophe Chambon 3,4Michel Hébraud Michel Hébraud 3,5Yann Guérardel Yann Guérardel 2Hang Thi Thu Nguyen Hang Thi Thu Nguyen 1Nicolas Barnich Nicolas Barnich 1
  • 1 Université Clermont Auvergne, Clermont-Ferrand, Auvergne, France
  • 2 UMR8576 Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), Villeneuve-d'Ascq, Nord-Pas-de-Calais, France
  • 3 Plateforme d’Exploration du Métabolisme, composante protéomique (PFEMcp), INRAE, Theix, France
  • 4 INRA UR370 Qualité des Produits Animaux, Theix, France
  • 5 INRA UMR0454 Microbiologie Environnement Digestif et Santé, Clermont-Ferrand, Auvergne, France

The final, formatted version of the article will be published soon.

    The Escherichia coli surfaceome consists mainly of the large surface organelles expressed by the organism to navigate and interact with the surrounding environment. The current study focuses on type I fimbriae and flagella. These large polymeric surface organelles are composed of hundreds to thousands of subunits, with their large size often preventing them from being studied in their native form. Recent studies are accumulating which demonstrate the glycosylation of surface proteins or virulence factors in pathogens, including E. coli. Using biochemical and glycobiological techniques, including biotin-hydrazide labelling of glycans and chemical and glycosidase treatments, we demonstrate i) the presence of a well-defined and chemically resistant FimA oligomer in several strains of pathogenic and non-pathogenic E. coli, ii) the major subunit of type I fimbriae, FimA, in pathogenic and laboratory strains is recognized by concanavalin A, iii) standard methods to remove N-glycans (PNGase F) or a broad-specificity mannosidase fail to remove the glycan structure, despite the treatments resulting in altered migration in SDS-PAGE, iv) PNGase F treatment results in a novel 32 kDa band recognized by anti-FliC antiserum.While the exact identity of the glycan(s) and their site of attachment currently elude detection by conventional glycomics/glycoproteomics, the current findings highlight a potential additional layer of complexity of the surface (glyco)proteome of the commensal or adhesive and invasive E. coli strains studied.

    Keywords: Type I fimbriae, Flagella, post-translational modification, pathobiont, Glycobiology, structural characterization, Escherichia coli

    Received: 07 Oct 2024; Accepted: 16 Jan 2025.

    Copyright: © 2025 Kavanaugh, SIVIGNON, Rossez, Chouit, Chambon, Hébraud, Guérardel, Nguyen and Barnich. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Devon William Kavanaugh, Université Clermont Auvergne, Clermont-Ferrand, 63006, Auvergne, France

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.