Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data

Joshi, Hiren J.; Harrison, Mathew J.; Schulz, Benjamin L.; Cooper, Catherine A.; Packer, Nicolle H.; Karlsson, Niclas G.

doi:10.1002/pmic.200300784

Cited by 113 publications

(83 citation statements)

References 32 publications

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“…Perhaps even more important, literally hundreds of minor glycans can be detected by MS analysis, but the subsequent annotation and verification of structure is prohibitive. However, progress for developing automatic methods of annotation with sophisticated algorithms is being made (65)(66)(67), and technology advances in sample preparation and analysis will rapidly evolve.…”

Section: Discussionmentioning

confidence: 99%

Activation of Murine CD4+ and CD8+ T Lymphocytes Leads to Dramatic Remodeling ofN-Linked Glycans

Comelli¹,

Sutton-Smith

Qi³

et al. 2006

The Journal of Immunology

114

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Differentiation and activation of lymphocytes are documented to result in changes in glycosylation associated with biologically important consequences. In this report, we have systematically examined global changes in N-linked glycosylation following activation of murine CD4 T cells, CD8 T cells, and B cells by MALDI-TOF mass spectrometry profiling, and investigated the molecular basis for those changes by assessing alterations in the expression of glycan transferase genes. Surprisingly, the major change observed in activated CD4 and CD8 T cells was a dramatic reduction of sialylated biantennary N-glycans carrying the terminal NeuGcα2-6Gal sequence, and a corresponding increase in glycans carrying the Galα1-3Gal sequence. This change was accounted for by a decrease in the expression of the sialyltransferase ST6Gal I, and an increase in the expression of the galactosyltransferase, α1-3GalT. Conversely, in B cells no change in terminal sialylation of N-linked glycans was evident, and the expression of the same two glycosyltransferases was increased and decreased, respectively. The results have implications for differential recognition of activated and unactivated T cells by dendritic cells and B cells expressing glycan-binding proteins that recognize terminal sequences of N-linked glycans.

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Section: Discussionmentioning

confidence: 99%

Activation of Murine CD4+ and CD8+ T Lymphocytes Leads to Dramatic Remodeling ofN-Linked Glycans

Comelli¹,

Sutton-Smith

Qi³

et al. 2006

The Journal of Immunology

114

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“…Structures were assigned if they had a segmentation score of 1 and 2 based on the algorithms used in this software. 9 Mass spectrometric relative intensities for comparison of individual oligosaccharides were obtained from summation of the intensities within a chromatographic peak of the isotopic cluster associated with each individual monoisotopic m/z corresponding to pseudomolecular ions of each detected oligosaccharide.…”

Section: Chemical Release Of O-linkedmentioning

confidence: 99%

Glycoproteomics of Milk: Differences in Sugar Epitopes on Human and Bovine Milk Fat Globule Membranes

Wilson¹,

Robinson

Donnet

et al. 2008

J. Proteome Res.

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Oligosaccharides from human and bovine milk fat globule membranes were analyzed by LC-MS and LC-MS/MS. Global release of N-linked and O-linked oligosaccharides showed both to be highly sialylated, with bovine peak-lactating milk O-linked oligosaccharides presenting as mono-and disialylated core 1 oligosaccharides (Gal 1-3GalNAcol), while human milk had core type 2 oligosaccharides (Gal 1-3(GlcNAc 1-6)GalNAcol) with sialylation on the C-3 branch. The C-6 branch of these structures was extended with branched and unbranched N-acetyllactosamine units terminating in blood group H and Lewis type epitopes. These epitopes were also presented on the reducing terminus of the human, but not the bovine, N-linked oligosaccharides. The O-linked structures were found to be attached to the high molecular mass mucins isolated by agarose-polyacrylamide composite gel electrophoresis, where MUC1 and MUC4 were present. Analysis of bovine colostrum showed that O-linked core 2 oligosaccharides are present at the early stage (3 days after birth) but are down-regulated as lactation develops. This data indicates that human milk may provide different innate immune protection against pathogens compared to bovine milk, as evidenced by the presence of Lewis b epitope, a target for the Helicobacter pylori bacteria, on human, but not bovine, milk fat globule membrane mucins. In addition, non-mucintype O-linked fucosylated oligosaccharides were found (NeuAc-Gal-GlcNAc1-3Fuc-ol in bovine milk and Gal-GlcNAc1-3Fuc-ol in human milk). The O-linked fucose structure in human milk is the first to our knowledge to be found on high molecular mass mucin-type molecules.

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“…In principle, however, it is di‹cult to determine anomeric (a, b) conˆgurations using such techniques. In this respect, several software programs and websites that assist complicated interpretation of fragment ion data are now available (13)(14)(15)(16)(17)(18). However, one of the major problems associated with this approach is that the necessary/desirable fragment information is not always obtained from, for example, the MS 2 and PSD spectra.…”

Section: B Ms-based Structural Analysis Of Glycansmentioning

confidence: 99%

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Deguchi

2008

TIGG

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Key Words: oligosaccharides, mass spectrometry, spectral library,glycopeptides A. IntroductionDNA sequences are now routinely analyzed by using highthroughput polymerase chain reaction (PCR) and DNA sequencers. Trace analyses of proteins are also being performed by combining highly selective and sensitive mass spectrometry (MS) with a universal protein database (e.g., SWISS-PROT) (1). However, for oligosaccharides (glycans), MS-based analysis continues to be associated with many di‹culties despite the fact that the molecular weights of glycans (a few hundred to a few thousand Daltons) are considerably smaller than are those of proteins and DNA. The reason for such di‹culties stems from the structural diversity of these molecules and the existence of structural isomers, the latter of which are inherent features of glycans that arise from various glycoside linkages, branching, anomeric (a, b) conˆgurations, and monosaccharide isomers. Isomers pose various problems for MS analysis, a technique that is based on the measurement of ion mass (m/z: mass-to-charge ratio). A further di‹culty is related to the heterogeneity of the N-and O-glycans attached to proteins There are, for example, 16 diŠerent types of neutral N-glycan associated with the human IgG protein (2). Consequently, the amount of each glycan is considerably smaller than that of the parent protein. Therefore, analysis of glycans requires an appreciably more sensitive MS and a much more meticulous sample preparation in order to minimize glycan loss (3-5).Last year, MS-based analytical methods for glycans and glycoproteins (i.e., glycomics and glycoproteomics) were widely reviewed in this journal (6,7). Although some duplication of this material is unavoidable, I would like to review the problems associated with current MS techniques, and in particular focus on the assignment of glycans based on MS n spectral database and matching. I will also brie‰y describe the future prospects for these techniques. B. MS-based structural analysis of glycansGlycans containing many hydroxyl groups are nonvolatile

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Development of a mass fingerprinting tool for automated interpretation of oligosaccharide fragmentation data

Cited by 113 publications

References 32 publications

Activation of Murine CD4+ and CD8+ T Lymphocytes Leads to Dramatic Remodeling ofN-Linked Glycans

Activation of Murine CD4+ and CD8+ T Lymphocytes Leads to Dramatic Remodeling ofN-Linked Glycans

Glycoproteomics of Milk: Differences in Sugar Epitopes on Human and Bovine Milk Fat Globule Membranes

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