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Int. J. Mol. Sci. 2016, 17(11), 1854; doi:10.3390/ijms17111854

Use of Atomic Force Microscopy to Study the Multi-Modular Interaction of Bacterial Adhesins to Mucins

1
The Gut Health and Food Safety Institute Strategic Programme, Institute of Food Research, Norwich Research Park, Norwich NR4 7UA, UK
2
Division of Neonatology and Division of Gastroenterology, Hepatology and Nutrition, Department of Pediatrics, School of Medicine, University of California San Diego, 9500 Gilman Drive, San Diego, CA 92093-0715, USA
*
Authors to whom correspondence should be addressed.
Academic Editor: Cheorl-Ho Kim
Received: 9 September 2016 / Revised: 26 October 2016 / Accepted: 2 November 2016 / Published: 8 November 2016
(This article belongs to the Special Issue Glycan–Receptor Interaction)
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Abstract

The mucus layer covering the gastrointestinal (GI) epithelium is critical in selecting and maintaining homeostatic interactions with our gut bacteria. However, the molecular details of these interactions are not well understood. Here, we provide mechanistic insights into the adhesion properties of the canonical mucus-binding protein (MUB), a large multi-repeat cell–surface adhesin found in Lactobacillus inhabiting the GI tract. We used atomic force microscopy to unravel the mechanism driving MUB-mediated adhesion to mucins. Using single-molecule force spectroscopy we showed that MUB displayed remarkable adhesive properties favouring a nanospring-like adhesion model between MUB and mucin mediated by unfolding of the multiple repeats constituting the adhesin. We obtained direct evidence for MUB self-interaction; MUB–MUB followed a similar binding pattern, confirming that MUB modular structure mediated such mechanism. This was in marked contrast with the mucin adhesion behaviour presented by Galectin-3 (Gal-3), a mammalian lectin characterised by a single carbohydrate binding domain (CRD). The binding mechanisms reported here perfectly match the particular structural organization of MUB, which maximizes interactions with the mucin glycan receptors through its long and linear multi-repeat structure, potentiating the retention of bacteria within the outer mucus layer. View Full-Text
Keywords: atomic force microscopy; single molecule force spectroscopy; intestinal mucin; mucus binding protein; bacterial adhesins; gut microbiota; Lactobacillus reuteri atomic force microscopy; single molecule force spectroscopy; intestinal mucin; mucus binding protein; bacterial adhesins; gut microbiota; Lactobacillus reuteri
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Gunning, A.P.; Kavanaugh, D.; Thursby, E.; Etzold, S.; MacKenzie, D.A.; Juge, N. Use of Atomic Force Microscopy to Study the Multi-Modular Interaction of Bacterial Adhesins to Mucins. Int. J. Mol. Sci. 2016, 17, 1854.

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