Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles

Latousakis, Dimitrios, Nepravishta, Ridvan, Rejzek, Martin, Wegmann, Udo, Le Gall, Gwenaelle, Kavanaugh, Devon, Colquhoun, Ian, Frese, Steven, MacKenzie, Donald, Walter, Jens, Angulo, Jesus, Field, Rob and Juge, Nathalie (2019) Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles. Glycobiology, 29 (1). pp. 45-58. ISSN 0959-6658

[thumbnail of Accepted manuscript]
Preview
PDF (Accepted manuscript) - Accepted Version
Available under License Creative Commons Attribution.

Download (398kB) | Preview
[thumbnail of Glycobiology_2019_Latousakis_etal]
Preview
PDF (Glycobiology_2019_Latousakis_etal) - Published Version
Available under License Creative Commons Attribution.

Download (967kB) | Preview

Abstract

Lactobacillus reuteri is a gut symbiont inhabiting the gastrointestinal tract of numerous vertebrates. The surface-exposed Serine-Rich Repeat Protein (SRRP) is a major adhesin in Gram-positive bacteria. Using lectin and sugar nucleotide profiling of wild-type or L. reuteri isogenic mutants, MALDI-ToF-MS, LC-MS and GC-MS analyses of SRRPs, we showed that L. reuteri strains 100-23C (from rodent) and ATCC 53608 (from pig) can perform protein O-glycosylation and modify SRRP100-23 and SRRP53608 with Hex-Glc-GlcNAc and di-GlcNAc moieties, respectively. Furthermore, in vivo glycoengineering in E. coli led to glycosylation of SRRP53608 variants with α-GlcNAc and GlcNAcβ(1→6)GlcNAcα moieties. The glycosyltransferases involved in the modification of these adhesins were identified within the SecA2/Y2 accessory secretion system and their sugar nucleotide preference determined by saturation transfer difference NMR spectroscopy and differential scanning fluorimetry. Together, these findings provide novel insights into the cellular O-protein glycosylation pathways of gut commensal bacteria and potential routes for glycoengineering applications.

Item Type: Article
Uncontrolled Keywords: chemistry,glycosylation,chemistry,mutation,nuclear magnetic resonance, biomolecular,repetitive sequences, amino acid
Faculty \ School: Faculty of Science > School of Pharmacy (former - to 2024)
Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
UEA Research Groups: Faculty of Medicine and Health Sciences > Research Centres > Lifespan Health
Faculty of Science > Research Groups > Pharmaceutical Materials and Soft Matter
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 26 Oct 2018 09:31
Last Modified: 06 Feb 2025 08:03
URI: https://ueaeprints.uea.ac.uk/id/eprint/68639
DOI: 10.1093/glycob/cwy100

Downloads

Downloads per month over past year

Actions (login required)

View Item View Item