Protein O-glucosylation in Lactobacillus buchneri

Anzengruber, Julia; Pabst, Martin; Neumann, Laura; Sekot, Gerhard; Heinl, Stefan; Grabherr, Reingard; Altmann, Friedrich; Messner, Paul; Schäffer, Christina

doi:10.1007/s10719-013-9505-7

Cited by 26 publications

(34 citation statements)

References 78 publications

(102 reference statements)

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“…Cell Division-Related Proteins A common trend in lactobacilli, which are known to glycosylate proteins, is the glycosylation of cell wall hydrolases like the Msp1 glycoprotein of L. rhamnosus GG and related autolysins and cell wall hydrolases in L. plantarum WCFS1 [Fredriksen et al, 2012;Rolain et al, 2013], Lactococcus lactis [Huard et al, 2003] and Lactococcus buchneri [Anzengruber et al, 2014]. In this work, the glycosylation of the cell wall hydrolase and probiotic effector Msp1 was further independently confirmed.…”

Section: Transporterssupporting

confidence: 60%

“…Indeed, in the major Gram-negative commensal Bacteroides fragilis, the general protein O -glycosylation system was shown to be essential for the competitive colonization of the mammalian intestine [Coyne et al, 2013;Fletcher et al, 2009Fletcher et al, , 2011, although specific interactions have not been mapped yet. Also, in several Gram-positive Lactobacillus strains, glycoproteins have been reported [Anzengruber et al, 2014;Fredriksen et al, 2012Fredriksen et al, , 2013Lebeer et al, 2012].…”

mentioning

confidence: 99%

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Systematic Exploration of the Glycoproteome of the Beneficial Gut Isolate Lactobacillus rhamnosus GG

Tytgat

Schoofs²,

Vanderleyden³

et al. 2016

Microb Physiol

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Glycoproteins form an interesting class of macromolecules involved in bacterial-host interactions, but they are not yet widely explored in Gram-positive and beneficial species. Here, an integrated and widely applicable approach was followed to identify putative bacterial glycoproteins, combining proteome fractionation with 2D protein and glycostained gels and lectin blots. This approach was validated for the microbiota isolate Lactobacillus rhamnosus GG. The approach resulted in a list of putative glycosylated proteins receiving a ‘glycosylation score'. Ultimately, we could identify 41 unique glycosylated proteins in L. rhamnosus GG (6 top-confidence, 10 high-confidence and 25 putative hits; classification based on glycosylation score). Most glycoproteins are associated with the cell wall and membrane. Identified glycoproteins include proteins involved in transport, translation, and sugar metabolism processes. A robust screening resulted in a comprehensive mapping of glycoproteins in L. rhamnosus GG. Our results reflect the glycosylation of sugar metabolism enzymes, transporters, and other proteins crucial for cell physiology. We hypothesize that protein glycosylation can confer an extra level of regulation, for example by affecting enzyme functions. This is the first systematic study of the glycoproteome of a probiotic and beneficial gut isolate.

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Section: Transporterssupporting

confidence: 60%

mentioning

confidence: 99%

Systematic Exploration of the Glycoproteome of the Beneficial Gut Isolate Lactobacillus rhamnosus GG

Tytgat

Schoofs²,

Vanderleyden³

et al. 2016

Microb Physiol

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“…Also, glycosylation of a PG hydrolase in L. rhamnosus GG, Lactobacillus plantarum WCFS1, and Lactococcus lactis MG1363 was reported (89,90,92). For Lactobacillus buchneri strains CD034 and NRRL, the glucosylation of putative glycosylhydrolases (LbGH25B and LbGH25N, respectively) was reported recently (93).…”

Section: Protein Glycosylationmentioning

confidence: 94%

“…PG cannot be viewed as merely a rigid structure, as the macromolecule is subjected to continuous expansion and turnover (83). This turnover is carried out by PG hydrolases, which, strikingly, are glycosylated in several species (see below) (89)(90)(91)(92)(93). PG is also modified after assembly in many species, and in Gram-positive species, the PG serves as a scaffold on which cell wall-associated molecules, such as TAs and CPS, are anchored (81,83).…”

Section: Figmentioning

confidence: 99%

The Sweet Tooth of Bacteria: Common Themes in Bacterial Glycoconjugates

Tytgat

Lebeer

2014

Microbiol Mol Biol Rev

128

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SUMMARY Humans have been increasingly recognized as being superorganisms, living in close contact with a microbiota on all their mucosal surfaces. However, most studies on the human microbiota have focused on gaining comprehensive insights into the composition of the microbiota under different health conditions (e.g., enterotypes), while there is also a need for detailed knowledge of the different molecules that mediate interactions with the host. Glycoconjugates are an interesting class of molecules for detailed studies, as they form a strain-specific barcode on the surface of bacteria, mediating specific interactions with the host. Strikingly, most glycoconjugates are synthesized by similar biosynthesis mechanisms. Bacteria can produce their major glycoconjugates by using a sequential or an en bloc mechanism, with both mechanistic options coexisting in many species for different macromolecules. In this review, these common themes are conceptualized and illustrated for all major classes of known bacterial glycoconjugates, with a special focus on the rather recently emergent field of glycosylated proteins. We describe the biosynthesis and importance of glycoconjugates in both pathogenic and beneficial bacteria and in both Gram-positive and -negative organisms. The focus lies on microorganisms important for human physiology. In addition, the potential for a better knowledge of bacterial glycoconjugates in the emerging field of glycoengineering and other perspectives is discussed.

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“…The glycosylation of surface (S-) layer proteins which cover the cell surface of a variety of bacterial species is a common modification of this class of proteins (25,26). The extensive MS analysis performed in mutant backgrounds on the S-layer proteins of Geobacillus stearothermophilus and Paenibacillus alvei have made possible the reconstruction of the biosynthesis pathway for S-layer glycans, and also to propose a model for their export and transfer to S-layer proteins (27,28). Interestingly, the P. alvei study also revealed that tyrosine residues can be modified by a bacterial protein glycosylation pathway (28).…”

mentioning

confidence: 99%

O-Glycosylation of the N-terminal Region of the Serine-rich Adhesin Srr1 of Streptococcus agalactiae Explored by Mass Spectrometry

Chaze

Guillot

Valot³

et al. 2014

Molecular & Cellular Proteomics

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Serine-rich (Srr) proteins exposed at the surface of Gram-positive bacteria are a family of adhesins that contribute to the virulence of pathogenic staphylococci and streptococci. Lectin-binding experiments have previously shown that Srr proteins are heavily glycosylated. We report here the first mass-spectrometry analysis of the glycosylation of Streptococcus agalactiae Srr1. After Srr1 enrichment and trypsin digestion, potential glycopeptides were identified in collision induced dissociation spectra using X! Tandem. The approach was then refined using higher energy collisional dissociation fragmentation which led to the simultaneous loss of sugar residues, production of diagnostic oxonium ions and backbone fragmentation for glycopeptides. This Protein glycosylation takes place in bacteria. A considerable amount of information on the biochemical pathways involved in protein glycosylation has been obtained in the genera Campylobacter and Neisseria (1-3). Hence, functional studies performed on Gram-negative bacteria have revealed important properties of protein glycosylation pathways. Like in eukaryotes, proteins can be glycosylated on asparagines (N-glycosylation) or serine/threonine residues (O-glycosylation). Two modes of glycan transfer onto proteins have been characterized in Gram-negative bacteria. In the first, the activated glycan is synthesized on a lipid carrier on the cytoplasmic side of the membrane. After membrane translocation, the glycan portion of the polyprenyl-phosphate-glycan intermediate is transferred en bloc to the protein by an oligosaccharyltransferase active in the periplasm. Such mechanism has been demonstrated for N-glycosylation in Campylobacter jejuni (4 -6) and O-glycosylation in Neisseria gonorrheae (7-9). These pathways are responsible for the glycosylation of more than 65 proteins in C. jejuni (10) and 12 different proteins in N.

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Protein O-glucosylation in Lactobacillus buchneri

Abstract: Abstract

Cited by 26 publications

References 78 publications

Systematic Exploration of the Glycoproteome of the Beneficial Gut Isolate <b><i>Lactobacillus rhamnosus </i></b>GG

Systematic Exploration of the Glycoproteome of the Beneficial Gut Isolate <b><i>Lactobacillus rhamnosus </i></b>GG

The Sweet Tooth of Bacteria: Common Themes in Bacterial Glycoconjugates

O-Glycosylation of the N-terminal Region of the Serine-rich Adhesin Srr1 of Streptococcus agalactiae Explored by Mass Spectrometry

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