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- Title
Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.
- Authors
Latousakis, Dimitrios; Nepravishta, Ridvan; Rejzek, Martin; Wegmann, Udo; Gall, Gwenaelle Le; Kavanaugh, Devon; Colquhoun, Ian J; Frese, Steven; MacKenzie, Donald A; Walter, Jens; Angulo, Jesus; Field, Robert A; Juge, Nathalie
- 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.
- Subjects
SERINE; LACTOBACILLUS reuteri; BACTERIAL adhesins; GLYCOSYLATION; LECTINS
- Publication
Glycobiology, 2019, Vol 29, Issue 1, p45
- ISSN
0959-6658
- Publication type
Article
- DOI
10.1093/glycob/cwy100