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

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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
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	26 Oct 2018 09:31
Last Modified:	24 May 2022 13:03
URI:	https://ueaeprints.uea.ac.uk/id/eprint/68639
DOI:	10.1093/glycob/cwy100

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