Structural basis for adaptation of lactobacilli to gastrointestinal mucus. (23rd January 2014)
- Record Type:
- Journal Article
- Title:
- Structural basis for adaptation of lactobacilli to gastrointestinal mucus. (23rd January 2014)
- Main Title:
- Structural basis for adaptation of lactobacilli to gastrointestinal mucus
- Authors:
- Etzold, Sabrina
Kober, Olivia I.
MacKenzie, Donald A.
Tailford, Louise E.
Gunning, A. Patrick
Walshaw, John
Hemmings, Andrew M.
Juge, Nathalie - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p>The mucus layer covering the gastrointestinal (GI) epithelium is critical in selecting and maintaining homeostatic interactions with our gut bacteria. However, the underpinning mechanisms of these interactions are not understood. Here, we provide structural and functional insights into the canonical mucus‐binding protein (MUB), a multi‐repeat cell‐surface adhesin found in <italic>L</italic><italic>actobacillus</italic> inhabitants of the GI tract. X‐ray crystallography together with small‐angle X‐ray scattering demonstrated a 'beads on a string' arrangement of repeats, generating 174 nm long protein fibrils, as shown by atomic force microscopy. Each repeat consists of tandemly arranged Ig‐ and mucin‐binding protein (MucBP) modules. The binding of full‐length MUB was confined to mucus via multiple interactions involving terminal sialylated mucin glycans. While individual MUB domains showed structural similarity to fimbrial proteins from Gram‐positive pathogens, the particular organization of MUB provides a structural explanation for the mechanisms in which lactobacilli have adapted to their host niche by maximizing interactions with the mucus receptors, potentiating the retention of bacteria within the mucus layer. Together, this study reveals functional and structural features which may affect tropism of microbes across mucus and along the GI tract, providing unique insights into the mechanisms adopted by commensals<abstract abstract-type="main"> <title>Summary</title> <p>The mucus layer covering the gastrointestinal (GI) epithelium is critical in selecting and maintaining homeostatic interactions with our gut bacteria. However, the underpinning mechanisms of these interactions are not understood. Here, we provide structural and functional insights into the canonical mucus‐binding protein (MUB), a multi‐repeat cell‐surface adhesin found in <italic>L</italic><italic>actobacillus</italic> inhabitants of the GI tract. X‐ray crystallography together with small‐angle X‐ray scattering demonstrated a 'beads on a string' arrangement of repeats, generating 174 nm long protein fibrils, as shown by atomic force microscopy. Each repeat consists of tandemly arranged Ig‐ and mucin‐binding protein (MucBP) modules. The binding of full‐length MUB was confined to mucus via multiple interactions involving terminal sialylated mucin glycans. While individual MUB domains showed structural similarity to fimbrial proteins from Gram‐positive pathogens, the particular organization of MUB provides a structural explanation for the mechanisms in which lactobacilli have adapted to their host niche by maximizing interactions with the mucus receptors, potentiating the retention of bacteria within the mucus layer. Together, this study reveals functional and structural features which may affect tropism of microbes across mucus and along the GI tract, providing unique insights into the mechanisms adopted by commensals and probiotics to adapt to the mucosal environment.</p> </abstract> … (more)
- Is Part Of:
- Environmental microbiology. Volume 16:Number 3(2014:Mar.)
- Journal:
- Environmental microbiology
- Issue:
- Volume 16:Number 3(2014:Mar.)
- Issue Display:
- Volume 16, Issue 3 (2014)
- Year:
- 2014
- Volume:
- 16
- Issue:
- 3
- Issue Sort Value:
- 2014-0016-0003-0000
- Page Start:
- 888
- Page End:
- 903
- Publication Date:
- 2014-01-23
- Subjects:
- Microbial ecology -- Periodicals
Environmental Microbiology -- Periodicals
579.17 - Journal URLs:
- http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1462-2912;screen=info;ECOIP ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920/issues ↗
http://www.blackwell-synergy.com/member/institutions/issuelist.asp?journal=emi ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/1462-2920.12377 ↗
- Languages:
- English
- ISSNs:
- 1462-2912
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3791.522600
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British Library HMNTS - ELD Digital store - Ingest File:
- 4031.xml