ArticleGlycobiology2019
Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.
Article in Glycobiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Origin and Evolution of Very Large Extracellular Proteins in Fructophilic Lactic Acid Bacteria.Genome biology and evolution · 2026Article
- Genome-wide association analysis reveals specialization to hosts and niches in multiple species of the Lactobacillaceae.The ISME journal · 2026Article
- Commensal bacterial glycosylation at the interface of host-bacteria interactions.Gut microbes · 2025Review
- A structural basis for the strain-dependent UDP-sugar specificity of glycosyltransferase C from the Limosilactobacillus reuteri accessory secretion system.Acta crystallographica. Section D, Structural biology · 2025Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- The role of the glycome in symbiotic host-microbe interactions.Glycobiology · 2023Review
- Glycosyltransferase 8 domain-containing protein 1 (GLT8D1) is a UDP-dependent galactosyltransferase.Scientific reports · 2023Article
- Impact of probiotic Limosilactobacillus reuteri DSM 17938 on amino acid metabolism in the healthy newborn mouse.Amino acids · 2022Article
- Quantifying and Engineering Mucus Adhesion of Probiotics.ACS synthetic biology · 2020Article
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- Streptococcal Serine-Rich Repeat Proteins in Colonization and Disease.Frontiers in microbiology · 2020Review
- O-acetylation controls the glycosylation of bacterial serine-rich repeat glycoproteins.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
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.
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Registered trials
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