Structural and molecular insights into novel surface-exposed mucus adhesins from Lactobacillus reuteri human strains:A novel mucus adhesin from Lactobacillus reuteri

Etzold, Sabrina, Mackenzie, Donald A., Jeffers, Faye, Walshaw, John, Roos, Stefan, Hemmings, Andrew M. ORCID: https://orcid.org/0000-0003-3053-3134 and Juge, Nathalie (2014) Structural and molecular insights into novel surface-exposed mucus adhesins from Lactobacillus reuteri human strains:A novel mucus adhesin from Lactobacillus reuteri. Molecular Microbiology, 92 (3). pp. 543-556. ISSN 0950-382X

Full text not available from this repository. (Request a copy)

Abstract

The mucus layer covering the gastrointestinal tract is the first point of contact of the intestinal microbiota with the host. Cell surface macromolecules are critical for adherence of commensal bacteria to mucus but structural information is scarce. Here we report the first molecular and structural characterization of a novel cell-surface protein, Lar_0958 from Lactobacillus reuteri JCM 1112(T) , mediating adhesion of L. reuteri human strains to mucus. Lar_0958 is a modular protein of 133 kDa containing six repeat domains, an N-terminal signal sequence and a C-terminal anchoring motif (LPXTG). Lar_0958 homologues are expressed on the cell-surface of L. reuteri human strains, as shown by flow-cytometry and immunogold microscopy. Adhesion of human L. reuteri strains to mucus in vitro was significantly reduced in the presence of an anti-Lar_0958 antibody and Lar_0958 contribution to adhesion was further confirmed using a L. reuteri ATCC PTA 6475 lar_0958 KO mutant (6475-KO). The X-ray crystal structure of a single Lar_0958 repeat, determined at 1.5 Å resolution, revealed a divergent immunoglobulin (Ig)-like β-sandwich fold, sharing structural homology with the Ig-like inter-repeat domain of internalins of the food borne pathogen Listeria monocytogenes. These findings provide unique structural insights into cell-surface protein repeats involved in adhesion of Gram-positive bacteria to the intestine.

Item Type:	Article
Additional Information:	© 2014 John Wiley & Sons Ltd.
Faculty \ School:	Faculty of Science > School of Chemistry Faculty of Science > School of Biological Sciences Faculty of Science > School of Computing Sciences Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Depositing User:	Pure Connector
Date Deposited:	09 Jun 2014 13:40
Last Modified:	24 Oct 2022 06:20
URI:	https://ueaeprints.uea.ac.uk/id/eprint/48592
DOI:	10.1111/mmi.12574

Actions (login required)

View Item