Latousakis, Dimitrios, Nepravishta, Ridvan, Rejzek, Martin, Wegmann, Udo, Le Gall, Gwenaelle ORCID: https://orcid.org/0000-0002-1379-2196, Kavanaugh, Devon, Colquhoun, Ian, Frese, Steven, MacKenzie, Donald, Walter, Jens, Angulo, Jesus ORCID: https://orcid.org/0000-0001-7250-5639, Field, Rob ORCID: https://orcid.org/0000-0001-8574-0275 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
Preview |
PDF (Accepted manuscript)
- Accepted Version
Available under License Creative Commons Attribution. Download (398kB) | Preview |
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: | 25 Sep 2024 13:42 |
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 |