Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles

Dimitrios Latousakis, Ridvan Nepravishta, Martin Rejzek, Udo Wegmann, Gwenaelle Le Gall, Devon Kavanaugh, Ian Colquhoun, Steven Frese, Donald MacKenzie, Jens Walter, Jesus Angulo, Rob Field, Nathalie Juge (Lead Author)

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)
21 Downloads (Pure)


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.
Original languageEnglish
Pages (from-to)45-58
Number of pages14
Issue number1
Early online date27 Oct 2018
Publication statusPublished - 1 Jan 2019


  • Adhesins, Bacterial/chemistry
  • Glycosylation
  • Lactobacillus reuteri/chemistry
  • Mutation
  • Nuclear Magnetic Resonance, Biomolecular
  • Repetitive Sequences, Amino Acid

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