Journal
GLYCOBIOLOGY
Volume 29, Issue 1, Pages 45-58Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwy100
Keywords
accessory secretion system; glycosyltransferase; gut commensal bacteria; O-linked glycosylation; sugar nucleotides
Categories
Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) Institute Strategic Programme for The Gut Health and Food Safety [BB/J004529/1]
- Biotechnology and Biological Sciences Research Council (BBSRC) Institute Strategic Programme for The Gut Microbes and Health [BB/R012490/1]
- Biotechnology and Biological Sciences Research Council (BBSRC) Institute Strategic Programmes for The Understanding and Exploiting Metabolism [BB/j004561/1]
- BBSRC [BB/P010660/1]
- John Innes Foundation
- Institute of Food Research (IFR)/Quadram Institute Bioscience (QIB) Extra
- BBSRC [BB/K019554/1, BBS/E/F/000PR10353, BBS/E/F/00044452, BB/P010660/1, BBS/E/F/000PR10356, BBS/E/F/000PR10355] Funding Source: UKRI
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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 -GlcNAc and GlcNAc(16)GlcNAc 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.
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