Advances in mass spectrometry‐based glycoproteomics

Abstract

Protein glycosylation, an important PTM, plays an essential role in a wide range of biological processes such as immune response, intercellular signaling, inflammation, and host–pathogen interaction. Aberrant glycosylation has been correlated with various diseases. However, studying protein glycosylation remains challenging because of low abundance, microheterogeneities of glycosylation sites, and poor ionization efficiency of glycopeptides. Therefore, the development of sensitive and accurate approaches to characterize protein glycosylation is crucial. The identification and characterization of protein glycosylation by MS is referred to as the field of glycoproteomics. Methods such as enrichment, metabolic labeling, and derivatization of glycopeptides in conjunction with different MS techniques and bioinformatics tools, have been developed to achieve an unequivocal quantitative and qualitative characterization of glycoproteins. This review summarizes the recent developments in the field of glycoproteomics over the past 6 years (2012 to 2018).

Biological Functions and Analytical Strategies of Sialic Acids in Tumor

“…Among those sugar analogues, Ac 4 ManNAz is mostly used as the azido group can be easily linked to probes or beads through click chemistry reaction. Sialic acid metabolic labeling combined with high resolution LC-MS offers simple detection in sialic acid modification sites of a certain protein [161]. As a result, analyzing the sialic acid modification in specific proteins enables researchers to explain the relationship between sialic acid modification and tumor progression in depth.…”

A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry–Based Glycoproteomics

“…MS-based Glycoproteomic Enrichment Strategies 8 analysis. We direct readers to prior reviews on glycoproteomic enrichment strategies for more historical perspectives (42-50), and we recommend several reviews that focus on N-or Oglycosylation classes more specifically (51)(52)(53)(54)(55)(56)(57)(58)(59). We also recognize recent reviews that more categorically address glycopeptide fragmentation methods (60)(61)(62), quantitative strategies for glycoproteomics (63,64), and informatics tools (65-69) -all of which make glycoproteomics an exciting and burgeoning field (70)(71)(72)(73).…”

Separation and detection of minimal length glycopeptide neoantigen epitopes centering the GSTA region of MUC1 by liquid chromatography/mass spectrometry

“…Significant progress has been made for glycopeptide analysis in the past decade. Databases and methods for analyzing N‐glycopeptides and O‐glycopeptides are accumulating, especially for site‐specific glycosylation. Obviously, data containing both identities of glycan structures and glycosylation sites are most valuable for their functional analysis, compared with data containing glycan structures or glycosylation sites alone.…”