Hexose Rearrangements upon Fragmentation of <i>N</i>-Glycopeptides and Reductively Aminated <i>N</i>-Glycans

Wuhrer, Manfred; Koeleman, Carolien A. M.; Deelder, André M.

doi:10.1021/ac900278q

Cited by 41 publications

(53 citation statements)

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“…fecalis. These assignments suggest that the observed variation in the hexose branch in the initial MS 2 analysis may be the result of terminal sugar re-arrangement during MS, as previously described (40). Although this suggests the identical group I mass glycan to be less variable than originally thought, the inability of NMR to detect the Hex-HexNAc-[Hex]-HexNAc 3 -diNAcBac glycan suggests low abundance glycan variability may still exist and is currently under investigation.…”

Section: Discussionsupporting

confidence: 52%

Diversity in the Protein N-Glycosylation Pathways Within the Campylobacter Genus

Nothaft

Scott

Vinogradov

et al. 2012

Molecular & Cellular Proteomics

158

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The foodborne bacterial pathogen, Campylobacter jejuni, possesses an N-linked protein glycosylation (pgl) pathway involved in adding conserved heptasaccharides to asparagine-containing motifs of >60 proteins, and releasing the same glycan into its periplasm as free oligosaccharides. In this study, comparative genomics of all 30 fully sequenced Campylobacter taxa revealed conserved pgl gene clusters in all but one species. Structural, phylogenetic and immunological studies showed that the N-glycosylation systems can be divided into two major groups. Group I includes all thermotolerant taxa, capable of growth at the higher body temperatures of birds, and produce the C. jejuni-like glycans. Within group I, the niche-adapted C. lari subgroup contain the smallest genomes among the epsilonproteobacteria, and are unable to glucosylate their pgl pathway glycans potentially reminiscent of the glucosyltransferase regression observed in the O-glycosylation system of Neisseria species. The nonthermotolerant Campylobacters, which inhabit a variety of hosts and niches, comprise group II and produce an unexpected diversity of N-glycan structures varying in length and composition. This includes the human gut commensal, C. hominis, which produces at least four different N-glycan structures, akin to the surface carbohydrate diversity observed in the well-studied commensal, Bacteroides. Both group I and II glycans are immunogenic and cell surface exposed, making these structures attractive targets for vaccine design and diagnostics. Molecular & Cellular Proteomics 11: 10.1074/mcp.M112.021519, 1203-1219, 2012.In eukaryotes, glycosylated proteins are ubiquitous components of extracellular matrices and cellular surfaces. Their oligosaccharide moieties are implicated in a wide variety of essential cell-cell and cell-matrix processes ranging from immune recognition to cancer development. The first general protein glycosylation (pgl) 1 pathway was discovered in the epsilonproteobacterium Campylobacter jejuni (1). The organism transfers a conserved heptasaccharide en bloc to asparagine residues within the sequon D/E-X 1 -N-X 2 -S/T (X 1 , X 2 P) of Ͼ60 glycoproteins (2-4). Furthermore, the pathway can be functionally transferred into Escherichia coli, and the oligosaccharyltransferase (OTase), PglB, is capable of adding foreign sugars to acceptor proteins (5-7). C. jejuni PglB also possesses hydrolase activity, influenced by the cellular growth phase and osmotic environment, releasing free oligosaccharides (fOS) into the periplasmic space in a 10:1 ratio relative to the amount of heptasaccharide N-linked to protein (8, 9).The C. jejuni N-linked heptasaccharide is conserved in structure in both C. jejuni and C. coli, the two most commonly isolated pathogenic Campylobacter species and major causes of human enteritis worldwide (10, 11). All campylobacters, but one, possess conserved pgl genes required for Nlinked protein glycosylation ((12) and this study). This posttranslational modification in C. jejuni influences DNA uptake, chicken and ...

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Section: Discussionsupporting

confidence: 52%

Diversity in the Protein N-Glycosylation Pathways Within the Campylobacter Genus

Nothaft

Scott

Vinogradov

et al. 2012

Molecular & Cellular Proteomics

158

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“…ternal saccharosamine residue (Shi et al, 1999) Interestingly, hexose rearrangements with loss of the penultimate GlcNAc residue, that is, the second GlcNAc counted from the labeled end, have been observed in MALDI-TOF/TOF-MS of oligomannosidic N-glycans labeled with 2AB and AA (Wuhrer, Koeleman, & Deelder, 2009) but not in MALDI-post-source decay (PSD)-TOF-MS of oligomannosidic N-glycans labeled with 4-aminobenzoic acid 2-(diethylamino)ethyl ester (Mo et al, 1998). Additional experiments are required to explain whether these observations are a result of the different physicochemical properties of the label or of the difference in energy deposition in the two MS-systems.…”

Section: A Reductively Aminated Glycansmentioning

confidence: 99%

Mass spectrometric glycan rearrangements

Wuhrer¹,

Deelder²,

Burgt³

2011

Mass Spectrometry Reviews

Self Cite

129

134

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Mass spectrometric rearrangement reactions have been reported for a large variety of compounds such as peptides, lipids, and carbohydrates. In the case of carbohydrates this phenomenon has been described as internal residue loss. Resulting fragment ions may be misinterpreted as fragments arising from conventional glycosidic bond cleavages, which may result in incorrect structural assignment. Therefore, awareness of the occurrence of glycan rearrangements is important for avoiding misinterpretation of tandem mass spectra. In this review mass spectrometric rearrangements of both derivatized and underivatized (native) oligosaccharide structures are discussed. Similar phenomena have been reported for glycopeptides, labeled glycan structures and other biomolecules containing a carbohydrate part. Rearrangements in oligosaccharides and glycoconjugates have been observed with different types of mass spectrometers. Most of the observed carbohydrate rearrangement reactions appear to be linked to the presence of a proton. Hence, tandem mass spectrometric analysis of alkali adducts or deprotonated ions often prevents rearrangement reactions, while they may happen with high efficacy with protonated glycoconjugates.

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“…However, the fragments indicated that fucose was linked to the first GlcNAc as well as to one of the mannoses. Proton adducts of fucosylated N-glycans are prone to fucose rearrangement, which gives rise to misleading fragments and therefore, the sodium adduct was selected for analysis by collision-induced decay (23,24). This yielded fragments unambiguously indicating the fucose to be linked to a mannose residue (Fig.…”

Section: Structural Characterization Of Chanterelle N-glycans By Massmentioning

confidence: 99%

Discovery and Structural Characterization of Fucosylated Oligomannosidic N-Glycans in Mushrooms

Grass

Pabst

Kolarich

et al. 2011

Journal of Biological Chemistry

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L-Fucose is a common constituent of Asn-linked glycans in vertebrates, invertebrates, and plants, but in fungal glycoproteins, fucose has not been found so far. However, by mass spectrometry we detected N-glycans and O-glycans containing one to six deoxyhexose residues in fruit bodies of several basidiomycetes. The N-glycans of chanterelles (Cantharellus cibarius) contained a deoxyhexose chromatographically identical to fucose and sensitive to ␣-L-fucosidase. Analysis of individual glycan species by tandem MS, glycosidase digestion, and finally 1 H NMR revealed the presence of L-fucose in ␣1,6-linkage to an ␣1,6-mannose of oligomannosidic N-glycans. The substitution by ␣1,6-mannose of ␣1,2-mannosyl residues of the canonical precursor structure was yet another hitherto unknown modification. No indication for the occurrence of yet other modifications, e.g. bisecting N-acetylglucosamine, was seen. Besides fucosylated N-glycans, short O-linked mannan chains substituted with fucose were present on chanterelle proteins. Although undiscovered so far, L-fucose appears to represent a prominent feature of protein-linked glycans in the fungal kingdom.The glycosylation capacity of fermentable yeasts and filamentous fungi has been well studied because of their potential biotechnological importance. In contrast to the members of other multicellular, eukaryotic organisms, i.e. green plants and metazoa, these fungi formed no complex-type N-glycans but rather oligomannosidic N-glycans often with characteristic extensions such as ␣1,3-mannose chains, phosphomannose or ␣-galactofuranose residues. This difference comfortably explains that fucose has so far not been found in fungal glycoproteins, as in animals and plants fucose occurs attached to N-acetylglucosamine (GlcNAc) or galactose residues in complex-type glycans only (1, 2). In fungi, fucose has only been detected in fungal polysaccharides (3-5) and in activated form as GDP-fucose (6) but not on protein-linked glycans.Fungi are classified into basal fungi and dikarya, which are further divided into ascomycota and basidiomycota. Agaricomycotina is one of the three subphyla of the basidiomycetes (7). With the exception of morels and truffles belonging to the ascomycetes, most of the fungal species with macroscopic fruiting bodies well known as -often edible -mushrooms are found in the phylum basidiomycota. Glycoproteins of three species of this group, i.e. Agaricus bisporus (8), Schizophyllum commune (9) and Coprinopsis cinerea (10) have been studied and found to contain exclusively regular oligomannosidic Nglycans. C. cinerea additionally contained glycans with a bisecting ␣1,4-GlcNAc residue (10).In this work, we studied the N-glycans of naturally growing mushrooms, in particular chanterelle (Cantharellus cibarius) by matrix assisted laser-desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). Surprisingly, many species exhibited oligomannosidic N-glycans, with a deoxyhexose, which, for chanterelles, was shown to be fucose ␣1,6-linked to mannose by tandem MS ...

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Hexose Rearrangements upon Fragmentation of N-Glycopeptides and Reductively Aminated N-Glycans

Cited by 41 publications

References 40 publications

Diversity in the Protein N-Glycosylation Pathways Within the Campylobacter Genus

Diversity in the Protein N-Glycosylation Pathways Within the Campylobacter Genus

Mass spectrometric glycan rearrangements

Discovery and Structural Characterization of Fucosylated Oligomannosidic N-Glycans in Mushrooms

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