Chain formation mediated by Escherichia coli immunoglobulin-binding proteins EibD and EibG depends on expression levels and localization of proteins

Swiatek, L-S, Schaufler, K and Leo, JC ORCID: https://orcid.org/0000-0002-7066-7527, 2025. Chain formation mediated by Escherichia coli immunoglobulin-binding proteins EibD and EibG depends on expression levels and localization of proteins. Scientific Reports, 15: 35244. ISSN 2045-2322

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Abstract

Escherichia coli expresses immunoglobulin-binding proteins (Eib), a subgroup of trimeric autotransporter adhesins (TAA). Subtypes of Eib proteins mediate unique chain-like adherence patterns and autoaggregation. This study investigates the mechanisms underlying chain formation by EibG and EibD; a chain-forming phenotype of the latter has not been previously described. Using constitutive expression systems, we demonstrate that moderate-level expression of EibG and EibD lead primarily to chain formation, whereas higher expression levels predominantly result in clump formation. Notably, chain and clump formation are not mutually exclusive and can occur simultaneously. Selective deletion of the full head domain, but not the N-terminal domain alone, abolished chain formation, highlighting its critical role. Fluorescence microscopy of mixed cultures showed that chains form through homotypic protein-protein interactions. Investigation revealed EibD and EibG were predominantly localized at cell poles, corresponding to sites of intercellular contact. Functional investigations showed that chain-forming strains exhibited enhanced adhesion to plastic surfaces, a key step in biofilm formation, without affecting autoaggregation. These showed Eib-mediated chain formation depends on protein expression levels, domain architecture, and localization, contributing to bacterial adhesion and potentially pathogenicity. Understanding interactions provides insights into TAA-mediated chain formation and autoaggregation.

Item Type:	Journal article
Publication Title:	Scientific Reports
Creators:	Swiatek, L.-S., Schaufler, K. and Leo, J.C.
Publisher:	Springer
Date:	9 October 2025
Volume:	15
ISSN:	2045-2322
Identifiers:	Number Type 10.1038/s41598-025-22967-3 DOI 2513718 Other
Rights:	This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
Divisions:	Schools > School of Science and Technology
Record created by:	Jonathan Gallacher
Date Added:	14 Oct 2025 13:48
Last Modified:	14 Oct 2025 13:48
URI:	https://irep.ntu.ac.uk/id/eprint/54565

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