The Major Autolysin Acm2 from Lactobacillus plantarum Undergoes Cytoplasmic O-Glycosylation

Fredriksen, Lasse; Mathiesen, Geir; Moen, Anders; Bron, Peter A.; Kleerebezem, Michiel; Eijsink, Vincent G. H.; Egge-Jacobsen, Wolfgang

doi:10.1128/jb.06314-11

Cited by 35 publications

(57 citation statements)

References 52 publications

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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: 99%

“…Glycosylated bacterial proteins have been characterized mainly in pathogens and include surface layer proteins, pilins, flagellins, and enzymes. Recent studies also reported the occurrence of glycoproteins in beneficial bacteria such as the gut symbiont Bacteroides fragilis (269,270) and Lactobacillus species (89,90,271).…”

Section: Protein Glycosylationmentioning

confidence: 99%

“…Glycosylation was recently shown to be an autoregulating factor of the enzyme and to have a negative impact on its N-acetylglucosaminidase activity. Twenty-one mono-GlcNAc substitutions were found in the AST domain of Acm2, which help to stabilize the enzyme against proteases (90,462). A broader screening of the glycoproteome of L. plantarum WCFS1 revealed 10 novel glycoproteins: 5 that have an intracellular nature, 2 extracellular PG hydrolases, and 1 mucus-binding protein.…”

Section: Protein Glycosylationmentioning

confidence: 99%

“…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%

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The Sweet Tooth of Bacteria: Common Themes in Bacterial Glycoconjugates

Tytgat

Lebeer

2014

Microbiol Mol Biol Rev

126

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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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Section: Protein Glycosylationmentioning

confidence: 99%

Section: Protein Glycosylationmentioning

confidence: 99%

Section: Protein Glycosylationmentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

See 2 more Smart Citations

The Sweet Tooth of Bacteria: Common Themes in Bacterial Glycoconjugates

Tytgat

Lebeer

2014

Microbiol Mol Biol Rev

126

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“…This glycosylation requires the concerted activities of two putative glycosyltransferases; Gtf1 and Gtf2 (37). More recent studies pinpointed that protein glycosylation also occurs in certain human intestine commensals, including several Bacteroides species (39,40), and probiotic species such as L. plantarum WCFS1 (41,42) and L. rhamnosus GG (43). More specifically, Msp1 of L. rhamnosus GG is O-glycosylated at serine residues 106 and 107, and its glycan moieties are recognized by the concanavalin A (ConA) lectin, which is specific for mannose and/or glucose moieties (43).…”

mentioning

confidence: 99%

GtfA and GtfB Are Both Required for Protein O -Glycosylation in Lactobacillus plantarum

et al. 2014

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e Acm2, the major autolysin of Lactobacillus plantarum WCFS1, was recently found to be O-glycosylated with N-acetylhexosamine, likely N-acetylglucosamine (GlcNAc). In this study, we set out to identify the glycosylation machinery by employing a comparative genomics approach to identify Gtf1 homologues, which are involved in fimbria-associated protein 1 (Fap1) glycosylation in Streptococcus parasanguinis. This in silico approach resulted in the identification of 6 candidate L. plantarum WCFS1 genes with significant homology to Gtf1, namely, tagE1 to tagE6. These candidate genes were targeted by systematic gene deletion, followed by assessment of the consequences on glycosylation of Acm2. We observed a changed mobility of Acm2 on SDS-PAGE in the tagE5E6 deletion strain, while deletion of other tagE genes resulted in Acm2 mobility comparable to that of the wild type. Subsequent mass spectrometry analysis of excised and in-gel-digested Acm2 confirmed the loss of glycosylation on Acm2 in the tagE5E6 deletion mutant, whereas a lectin blot using GlcNAc-specific succinylated wheat germ agglutinin (sWGA) revealed that besides Acm2, tagE5E6 deletion also abolished all but one other sWGA-reactive, protease-sensitive signal. Only complementation of both tagE5 and tagE6 restored those sWGA lectin signals, establishing that TagE5 and TagE6 are both required for the glycosylation of Acm2 as well as the vast majority of other sWGA-reactive proteins. Finally, sWGA lectin blotting experiments using a panel of 8 other L. plantarum strains revealed that protein glycosylation is a common feature in L. plantarum strains. With the establishment of these enzymes as protein glycosyltransferases, we propose to rename TagE5 and TagE6 as GtfA and GtfB, respectively.

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Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O‐GlcNAc)

Zachara

2018

FEBS Letters

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Almost 100 years after the first descriptions of proteins conjugated to carbohydrates (mucins), several studies suggested that glycoproteins were not restricted to the serum, extracellular matrix, cell surface, or endomembrane system. In the 1980’s, key data emerged demonstrating that intracellular proteins were modified by monosaccharides of O-linked β-N-acetylglucosamine (O-GlcNAc). Subsequently, this modification was identified on thousands of proteins that regulate cellular processes as diverse as protein aggregation, localization, post-translational modifications, activity, and interactions. In this Review, we will highlight critical discoveries that shaped our understanding of the molecular events underpinning the impact of O-GlcNAc on protein function, the role that O-GlcNAc plays in maintaining cellular homeostasis, and our understanding of the mechanisms that regulate O-GlcNAc-cycling.

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The Major Autolysin Acm2 from Lactobacillus plantarum Undergoes Cytoplasmic O-Glycosylation

Cited by 35 publications

References 52 publications

The Sweet Tooth of Bacteria: Common Themes in Bacterial Glycoconjugates

The Sweet Tooth of Bacteria: Common Themes in Bacterial Glycoconjugates

GtfA and GtfB Are Both Required for Protein O -Glycosylation in Lactobacillus plantarum

Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O‐GlcNAc)

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