Bacterial Protein N-Glycosylation: New Perspectives and Applications

Nothaft, Harald; Szymanski, Christine M.

doi:10.1074/jbc.r112.417857

Cited by 144 publications

(129 citation statements)

References 90 publications

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“…A majority of the bacterial glycoproteins identified so far are localized at the cell-surface where they are involved in a variety of processes such as biofilm formation, adhesion, cell motility, or immune system escape (2,79,81). In Bacteroides fragilis, a Gram-negative human symbiont, the general O-glycosylation system is involved in the modification of tens of proteins, contributes to in vitro fitness of the species and is also required for the colonization of the mammalian gastrointestinal gut (82,83).…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

“…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)(2)(3). Hence, functional studies performed on Gram-negative bacteria have revealed important properties of protein glycosylation pathways.…”

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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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“…Archaea and Eubacteria use their own sets of glycotransferases to assemble distinct oligosaccharides on their unique lipid-phospho carriers (2,11). Consequently, wide diversity is observed in the archaeal and eubacterial N-glycan structures, in terms of the sizes, compositions, branching patterns, and chemical modifications of the constituent monosaccharides (1,12).…”

mentioning

confidence: 99%

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Taguchi

Fujinami

Kohda

2016

Journal of Biological Chemistry

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The glycosylation of asparagine residues is the predominant protein modification in all three domains of life. An oligosaccharide chain is preassembled on a lipid-phospho carrier and transferred onto asparagine residues by the action of a membrane-bound enzyme, oligosaccharyltransferase. The oligosaccharide donor for the oligosaccharyl transfer reaction is dolichol-diphosphate-oligosaccharide in Eukaryota and polyprenol-diphosphate-oligosaccharide in Eubacteria. The donor in some archaeal species was reportedly dolichol-monophosphate-oligosaccharide. Thus, the difference in the number of phosphate groups aroused interest in whether the use of the dolichol-monophosphate type donors is widespread in the domain Archaea. Currently, all of the archaeal species with identified oligosaccharide donors have belonged to the phylum Euryarchaeota. Here, we analyzed the donor structures of two species belonging to the phylum Crenarchaeota, Pyrobaculum calidifontis and Sulfolobus solfataricus, in addition to two species from the Euryarchaeota, Pyrococcus furiosus and Archaeoglobus fulgidus. The electrospray ionization tandem mass spectrometry analyses confirmed that the two euryarchaeal oligosaccharide donors were the dolichol-monophosphate type and newly revealed that the two crenarchaeal oligosaccharide donors were the dolichol-diphosphate type. This novel finding is consistent with the hypothesis that the ancestor of Eukaryota is rooted within the TACK (Thaum-, Aig-, Cren-, and Korarchaeota) superphylum, which includes Crenarchaea. Our comprehensive study also revealed that one archaeal species could contain two distinct oligosaccharide donors for the oligosaccharyl transfer reaction. The A. fulgidus cells contained two oligosaccharide donors bearing oligosaccharide moieties with different backbone structures, and the S. solfataricus cells contained two oligosaccharide donors bearing stereochemically different dolichol chains.The glycosylation of asparagine residues is the predominant protein modification throughout all three domains of life (1-3). The oligosaccharides attached to asparagine residues in glycoproteins (N-glycan) affect various properties of the proteins, including folding, conformation, solubility, and antigenicity. Carbohydrate-binding proteins, such as lectins, recognize the N-glycans. Within the lumen of the endoplasmic reticulum in eukaryotic cells, the N-glycan functions as a quality control tag in the endoplasmic reticulum-associated degradation (4). The N-glycosylation occurs in the consensus motif (referred to as the sequon) represented by Asn-Xaa-Ser/Thr, where Xaa can be any residue except Pro. The formation of the N-glycosidic bond, between the monosaccharide residue at the reducing end of an oligosaccharide and the side chain amide group of the asparagine residues in proteins, is catalyzed by a membranebound enzyme, oligosaccharyltransferase (OST) 2 (3). The eukaryotic OST enzyme is a multisubunit protein complex. Among the eight different membrane subunit proteins, the catalytic subunit is a po...

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“…Such kindThis type of heterogeneity is likely to be present in different organisms of a species also. In one related study, it was established that glycan structures with different chain length are present in the genus Campylobacter when grouped on the basis of thermotolerance [44]. The variation of homologs in different organisms is not surprising since, even among Neisseria, species-and strain-specific polymorphisms have been reported [20,45].…”

Section: Resultsmentioning

confidence: 99%

Diversity, Abundance and Distribution of O-linked Glycosylation Pathway Enzymes in Prokaryotes-A Comparative Genomics Study

Balajia¹

2014

J Glycomics Lipidomics

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Bacterial Protein N-Glycosylation: New Perspectives and Applications

Cited by 144 publications

References 90 publications

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

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

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Diversity, Abundance and Distribution of O-linked Glycosylation Pathway Enzymes in Prokaryotes-A Comparative Genomics Study

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