Distinguishing phosphorylation and sulfation in carbohydrates and glycoproteins using ion-pairing and mass spectrometry

Zhang, Ying; Jiang, Hui; Go, Eden P.; Desaire, Heather

doi:10.1016/j.jasms.2006.05.013

Cited by 24 publications

(21 citation statements)

References 25 publications

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“…The analysis was performed according to a protocol by Zhang et al (25). Briefly, trilysine was dissolved in methanol/water (1:1) containing 0.5% acetic acid.…”

Section: Esi-ms/ms Of Lysine-glycan Ion Pairing-mentioning

confidence: 99%

“…Due to differences in the chemical bond stabilities it is possible to discriminate between sulfate and phosphate modifications by different MS 2 fragmentation patterns of the ion-pairing complexes (25). We performed MS 2 of the precursor ion at m/z 1401.8, a complex of tetralysine and the (sulfate-or phosphate-modified) core 2-tetrasaccharide alditol GalNAc1-4GlcNAc1-6(Gal1-3)GalNAc-ol derived from hDG8 (HN 3 P-K 4 ).…”

Section: Msmentioning

confidence: 99%

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O-Linked N,N′-Diacetyllactosamine (LacdiNAc)-modified Glycans in Extracellular Matrix Glycoproteins Are Specifically Phosphorylated at Subterminal N-Acetylglucosamine

Breloy

Pacharra

Ottis

et al. 2012

Journal of Biological Chemistry

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“…The analysis was performed according to a protocol by Zhang et al (25). Briefly, trilysine was dissolved in methanol/water (1:1) containing 0.5% acetic acid.…”

Section: Esi-ms/ms Of Lysine-glycan Ion Pairing-mentioning

confidence: 99%

Section: Msmentioning

confidence: 99%

O-Linked N,N′-Diacetyllactosamine (LacdiNAc)-modified Glycans in Extracellular Matrix Glycoproteins Are Specifically Phosphorylated at Subterminal N-Acetylglucosamine

Breloy

Pacharra

Ottis

et al. 2012

Journal of Biological Chemistry

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“…Although they have yet to be used in IMS studies, Desaire and coworkers have shown that ion-pairing reagents can be used to bind and ionize certain functionalized (e.g., phosphorylated or sulfated) saccharide species [21,22]. Due to the acidity of these functional groups, such ion-pairing reagents are typically oligomers of basic amino acid residues, such as trilysine [22].…”

Section: Introductionmentioning

confidence: 99%

“…Due to the acidity of these functional groups, such ion-pairing reagents are typically oligomers of basic amino acid residues, such as trilysine [22]. These reagents make it possible to differentiate between phosphorylated and sulfated species based on characteristic fragment ions produced upon collision-induced dissociation [21].…”

Section: Introductionmentioning

confidence: 99%

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

Bohrer

Clemmer

2011

J. Am. Soc. Mass Spectrom.

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The binding properties of a peptidoglycan recognition protein are translated via combinatorial chemistry into short peptides. Non-adjacent histidine, tyrosine, and arginine residues in the protein's binding cleft that associate specifically with the glycan moiety of a peptidoglycan substrate are incorporated into linear sequences creating a library of 27 candidate tripeptide reagents (three possible residues permutated across three positions). Upon electrospraying the peptide library and carbohydrate mixtures, some noncovalent complexes are observed. The binding efficiencies of the peptides vary according to their amino acid composition as well as the disaccharide linkage and carbohydrate ring-type. In addition to providing a charge-carrier for the carbohydrate, peptide reagents can also be used to differentiate carbohydrate isomers by ion mobility spectrometry. The utility of these peptide reagents as a means of enhancing ion mobility analysis of carbohydrates is illustrated by examining four glucose-containing disaccharide isomers, including a pair that is not resolved by ion mobility alone. The specificity and stoichiometry of the peptide-carbohydrate complexes are also investigated. Trihistidine demonstrates both suitable binding efficiency and successful resolution of disaccharides isomers, suggesting it may be a useful reagent in IMS analyses of carbohydrates.

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“…However, site-specificity is lost when releasing the glycan. In positive ion mode, ion-pairing reagents can be used to stabilise labile Sulf substituents on glycopeptides before direct infusion into the mass spectrometer (344). The use of lower dissociation energies in positive ion mode has been used for the characterisation of enriched O-linked glycopeptides containing sulfated glycosaminoglycan chains (238,267).…”

Section: Discussionmentioning

confidence: 99%

Structural characterisation of glycosylation of paramyxovirus attachment and fusion proteins by mass spectrometry

Pegg¹

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The family Paramyxoviridae (paramyxovirus) contains several significant human and animal pathogens.Represented within this family are human respiratory syncytial virus (hRSV) and Newcastle disease virus (NDV). The former contributes significantly to severe respiratory tract disease in infants, children and immunocompromised individuals. At present, highly efficacious therapeutics or safe and effective vaccines are not available for hRSV. NDV is the causative agent of Newcastle disease, afflicting a wide range of avian species. The desire to study NDV is due not only to the significant economic impact it has on the poultry industry worldwide, but also its potential use as an oncolytic agent and vaccine vector in humans and animals. Additionally, findings on NDV may be translated to closely related viruses that cause disease in humans, such as parainfluenza viruses.As outlined in Chapter 1 of this thesis, the infectious processes of all members of this family are driven by two major membrane glycoproteins whose ectodomains project from the viral envelope: the fusion (F) and attachment glycoproteins. The F glycoprotein is responsible for viral entry by means of fusion with host cell membranes while the variable attachment glycoproteins, haemagglutinin, haemagglutininneuraminidase (HN) and major surface glycoprotein (G), are involved in viral attachment to host cells.Previous studies have shown that altering the glycosylation profile of these proteins can modulate the ability of the virus to infect host cells and stimulate the host immune system. As yet, site-specific glycan heterogeneity of hRSV and NDV surface glycoproteins has not been defined at a chemical level. As described in Chapter 2, reverse-phase liquid chromatography tandem mass spectrometry (MS) strategies were implemented to characterise intact glycopeptides from the attachment and F glycoproteins of hRSV and NDV. Site-occupancy and monosaccharide compositions at a given site were determined using collision-induced dissociation, higher-energy collision dissociation, electron-transfer dissociation and electron-transfer dissociation combined with collision dissociation. As described in Chapter 3, a spectral processing program was developed called OxoExtract to aid identification of intact glycopeptides that were fragmented with higher-energy collision dissociation.The F and HN proteins of NDV were derived from virions propagated in embryonic eggs. Analyses of HN in Chapter 4 revealed high mannose N-linked glycans and complex or hybrid N-linked glycans that were variably fucosylated, sialylated and sulfated or phosphorylated. In total 63, 58, and 37 glycans were identified at sites N341, N433 and N481, respectively. In addition, a previously undocumented Olinked glycosylation site was identified in the stalk domain of the protein. Observed glycans from NDV F described in Chapter 5 were mainly high mannose, containing variations of five to nine mannose ii residues across four sites, N85, N191, N366 and N471. There was also evidence of fucosylated c...

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Distinguishing phosphorylation and sulfation in carbohydrates and glycoproteins using ion-pairing and mass spectrometry

Cited by 24 publications

References 25 publications

O-Linked N,N′-Diacetyllactosamine (LacdiNAc)-modified Glycans in Extracellular Matrix Glycoproteins Are Specifically Phosphorylated at Subterminal N-Acetylglucosamine

O-Linked N,N′-Diacetyllactosamine (LacdiNAc)-modified Glycans in Extracellular Matrix Glycoproteins Are Specifically Phosphorylated at Subterminal N-Acetylglucosamine

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

Structural characterisation of glycosylation of paramyxovirus attachment and fusion proteins by mass spectrometry

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