Carbohydrates on Proteins: Site-Specific Glycosylation Analysis by Mass Spectrometry

Zhu, Zhongkui; Desaire, Heather

doi:10.1146/annurev-anchem-071114-040240

Cited by 72 publications

(67 citation statements)

References 127 publications

(143 reference statements)

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“…Protein glycosylation is a site‐specific modification. The analysis of site‐specific glycosylation is important to reveal the structure‐function relationship of glycoproteins . MS‐based glycoproteomic techniques in combination with various sample preparation workflows have made great contributions in the field.…”

Section: Glycopeptidesmentioning

confidence: 99%

Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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Sialic acids are a family of structurally unique and negatively charged nine-carbon sugars, normally found at the terminal positions of glycan chains on glycoproteins and glycolipids. The glycosylation of proteins is a universal post-translational modification in eukaryotic species and regulates essential biological functions, in which the most common sialic acid is N-acetyl-neuraminic acid (2-keto-5-acetamido-3,5-dideoxy-D-glycero-D-galactononulopyranos-1-onic acid) (Neu5NAc). Because of the properties of sialic acids under general mass spectrometry (MS) conditions, such as instability, ionization discrimination, and mixed adducts, the use of MS in the analysis of protein sialoglycosylation is still challenging. The present review is focused on the application of MS related methodologies to the study of both N- and O-linked sialoglycans. We reviewed MS-based strategies for characterizing sialylation by analyzing intact glycoproteins, proteolytic digested glycopeptides, and released glycans. The review concludes with future perspectives in the field.

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Section: Glycopeptidesmentioning

confidence: 99%

Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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“…The ideal way to comprehensively characterize glycopeptides, especially in a large-scale glycoproteomics context, is to preserve the glycan side chain on the peptide and collect glycan and peptide fragmentation information simultaneously [13, 14]. However, due to its heterogeneous nature, fragmenting an intact glycopeptide has always been difficult and yet no single fragmentation technique is able to generate a complete picture in a single MS/MS spectrum [6, 7, 14, 15].…”

Section: Introductionmentioning

confidence: 99%

Electron-Transfer/Higher-Energy Collision Dissociation (EThcD)-Enabled Intact Glycopeptide/Glycoproteome Characterization

Wang

Chen

et al. 2017

J. Am. Soc. Mass Spectrom.

175

195

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Protein glycosylation, one of the most heterogeneous post-translational modifications, can play a major role in cellular signal transduction and disease progression. Traditional mass spectrometry (MS)-based large-scale glycoprotein sequencing studies heavily rely on identifying enzymatically released glycans and their original peptide backbone separately, as there is no efficient fragmentation method to produce unbiased glycan and peptide product ions simultaneously in a single spectrum and can be conveniently applied to high throughput glycoproteome characterization, especially for N-glycopeptides which can have much more branched glycan side chains than relatively less complex O-linked glycans. In this study a re-defined electron-transfer/higher-energy collision dissociation (EThcD) fragmentation scheme is applied to incorporate both glycan and peptide fragments in one single spectrum, enabling complete information to be gathered and great microheterogeneity details to be revealed. Fetuin was first utilized to prove the applicability with 19 glycopeptides and corresponding 5 glycosylation sites identified. Subsequent experiments tested its utility for human plasma N-glycoproteins. Large-scale studies explored N-glycoproteomics in rat carotid over the course of restenosis progression to investigate potential role of glycosylation. The integrated fragmentation scheme provides a powerful tool for the analysis of intact N-glycopeptides and N-glycoproteomics. We also anticipate this approach can be readily applied to large-scale O-glycoproteome characterization.

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“…Over the past few years, several published articles have reviewed the analytical methods developed for the characterization of glycans and glycoproteins with focus on chromatography, electrophoresis, electrochemistry, and MS [2][3][4][8][9][10][11][12][13][14][15][16]. This review specifically summarizes and highlights recent developments (2014)(2015)(2016) in the fields of glycomics and glycoproteomics with emphasis on the latest advancements involving MS imaging (MSI), ion mobility (IM) MS, and capillary separations.…”

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confidence: 99%

Recent advances in mass spectrometric analysis of glycoproteins

et al. 2016

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Glycosylation is one of the most common post-translational modifications of proteins and plays essential roles in various biological processes, including protein folding, host-pathogen interaction, immune response, and inflammation and aberrant protein glycosylation is a well-known event in various disease states including cancer. As a result, it is critical to develop rapid and sensitive methods for the analysis of abnormal glycoproteins associated with diseases. Mass spectrometry in conjugation with different separation methods, such as capillary electrophoresis, ion mobility, and high performance liquid chromatography, has become a popular tool for glycoprotein analysis, providing highly informative fragments for structural identification of glycoproteins. This review provides an overview of the developments and accomplishments in the field of glycomics and glycoproteomics reported between 2014 and 2016.

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Carbohydrates on Proteins: Site-Specific Glycosylation Analysis by Mass Spectrometry

Cited by 72 publications

References 127 publications

Mass spectrometry for protein sialoglycosylation

Mass spectrometry for protein sialoglycosylation

Electron-Transfer/Higher-Energy Collision Dissociation (EThcD)-Enabled Intact Glycopeptide/Glycoproteome Characterization

Recent advances in mass spectrometric analysis of glycoproteins

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