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

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 t...

Celý popis

Uložené v:

Podrobná bibliografia
Vydané v:	International journal of molecular sciences Ročník 17; číslo 11; s. 1854
Hlavní autori:	Gunning, A., Kavanaugh, Devon, Thursby, Elizabeth, Etzold, Sabrina, MacKenzie, Donald, Juge, Nathalie
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	Switzerland MDPI AG 08.11.2016 MDPI
Predmet:	Adhesins, Bacterial - chemistry Adhesins, Bacterial - isolation & purification Adhesins, Bacterial - metabolism Animals Bacteria Bacterial Adhesion Binding sites Cell adhesion & migration Culture Media, Conditioned - chemistry Galectin 3 - chemistry Galectin 3 - genetics Galectin 3 - metabolism Gene Expression Humans Intestinal Mucosa - chemistry Lactobacillus Limosilactobacillus reuteri - growth & development Limosilactobacillus reuteri - metabolism Microscopy Microscopy, Atomic Force Models, Molecular Mucin-3 - chemistry Mucin-3 - isolation & purification Mucin-3 - metabolism Protein Binding Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Swine intestinal mucin Lactobacillus reuteri single molecule force spectroscopy bacterial adhesins mucus binding protein atomic force microscopy gut microbiota
ISSN:	1422-0067, 1661-6596, 1422-0067
On-line prístup:	Získať plný text
Tagy:	Pridať tag Žiadne tagy, Buďte prvý, kto otaguje tento záznam!

Popis
Shrnutí:	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.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	1422-0067 1661-6596 1422-0067
DOI:	10.3390/ijms17111854