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Detection of Food Allergen Residues by Immunoassays and Mass Spectrometry
Published in Andreas L. Lopata, Food Allergy, 2017
Sridevi Muralidharan, Yiqing Zhao, Steve L. Taylor, Nanju A. Lee
Although glycoproteomics studies on milk and peanuts are gaining momentum, many of the known allergens lack such analysis which warrants glycoproteomic research towards further understanding. Together this has the potential to elucidate the properties of the allergenic moiety and could help in accurate food allergen management such as the development of more sensitive and specific allergen detection assays.
Proteomics Approaches to Uncover the Drug Resistance Mechanisms of Microbial Biofilms
Published in Chaminda Jayampath Seneviratne, Microbial Biofilms, 2017
Chaminda Jayampath Seneviratne, Tanujaa Suriyanarayanan, Lin Qingsong, Juan Antonio Vizcaíno
In recent years, a considerable number of glycoproteomics studies have been performed [155]. Glycoproteomics is gaining popularity for the study of prokaryotic organisms, as glycosylation contributes to the virulence of many bacterial pathogens [156]. This type of study has been performed on some fungi as well [157].
Glycosylation and its implications in breast cancer
Published in Expert Review of Proteomics, 2019
Danielle A. Scott, Richard R. Drake
The methodologies used for glycomic and glycoproteomic analysis have varied over the last 40 years, and have continued to improve. Much of the new capabilities for direct analysis of the glycans and glycoproteins have evolved with increasingly higher resolution and sensitive mass spectrometry approaches. A recent review highlights the many approaches that are being used [145]. In relation to breast cancer targets, these approaches have been limited. Two approaches recently published [21,146] highlight the feasibility of glycan and glycoprotein analysis. In one approach [146], multiple frozen tissue specimens from triple-negative and luminal (HER2-/ER+/PR+) tumor subtypes were homogenized and digested to the peptide level for subsequent capture of glycopeptides by an established hydrazine bead capture method. Hydrazine will react covalently with oxidized sugars on the glycopeptide. The attached peptides can then be released by treating with PNGase F, and then sequenced by LC-MS methods to identify the formerly glycosylated peptides [147]. Using this approach with label-free LC-MS, over 2000 bead-captured proteins were identified; 90 glycoproteins were differentially detected in higher abundance in triple-negative tumors relative to luminal tumors, and 86 glycoproteins were in higher abundance in the luminal tumor tissues [146]. Further analysis indicated that a subset of 29 glycoproteins in higher abundance in the triple-negative tumors could be used with public database transcriptomic data to distinguish triple-negative from luminal tumors, as well as be predictive for patient survival [146].
Mass spectrometry analysis of glycoprotein biomarkers in human blood of hepatocellular carcinoma
Published in Expert Review of Proteomics, 2019
Kwang Hoe Kim, Jin Young Kim, Jong Shin Yoo
Glycoproteins are differentially regulated in various cancers, which can provide diagnostic information. Abnormal levels of glycoproteins or altered glycosylation have been identified in various types of cancer [7]. Indeed, glycoproteins comprise the majority of biomarkers used in clinical studies [104]. An overall workflow for a development of glycoprotein biomarkers by MS-based glycoproteomic approaches is shown in Figure 1. The analysis of intact glycoproteins requires no sample preparations such as enzymatic digestion prior to MS analysis [105]. Peptides which have not any modification sites are most common and easily detected by MS. An analysis of chemical or enzymatic released glycans from the glycoprotein can be used to confirm the exact glycan structure. A glycopeptides derived from proteolytic digestion of the glycoprotein is most advantageous analyte to confirm peptide amino acid sequence and site-specific glycoforms.
Characterizing bacterial glycoproteins with LC-MS
Published in Expert Review of Proteomics, 2018
Kelly M. Fulton, Jianjun Li, Juan M. Tomas, Jeffrey C. Smith, Susan M. Twine
Proteomics is usually understood to be the large-scale identification and characterization of the complement of proteins within a cell or system. Glycoproteomics is a subdiscipline of proteomics, focusing on the complement of glycosylated proteins. Mass spectrometry (MS) and allied approaches have become the main technologies used for proteomic and glycoproteomic studies alike. The non-template driven nature of glycans, in combination with variability of glycoforms and modification sites, often necessitates a deeper, more focused study of discrete glycoproteins or glycopeptides, rather than large-scale glycoproteomic studies. The study of glycosylation in eukaryotic and bacterial organisms relies upon some common analytical approaches. However, for reasons that will be describe herein, bacterial glycoprotein analyses often necessitate different, novel, or more in-depth approaches. This review describes the current state-of-the-art for bacterial glycoprotein/glycopeptide analysis.