Determination of the glycoprotein specificity of lectins on cell membranes through oxidative proteomics.

Chemical Science
Yixuan XieCarlito B Lebrilla

Abstract

The cell membrane is composed of a network of glycoconjugates including glycoproteins and glycolipids that presents a dense matrix of carbohydrates playing critical roles in many biological processes. Lectin-based technology has been widely used to characterize glycoconjugates in tissues and cell lines. However, their specificity toward their putative glycan ligand and sensitivity in situ have been technologically difficult to study. Additionally, because they recognize primarily glycans, the underlying glycoprotein targets are generally not known. In this study, we employed lectin proximity oxidative labeling (Lectin PROXL) to identify cell surface glycoproteins that contain glycans that are recognized by lectins. Commonly used lectins were modified with a probe to produce hydroxide radicals in the proximity of the labeled lectins. The underlying polypeptides of the glycoproteins recognized by the lectins are oxidized and identified by the standard proteomic workflow. As a result, approximately 70% of identified glycoproteins were oxidized in situ by all the lectin probes, while only 5% of the total proteins were oxidized. The correlation between the glycosites and oxidation sites demonstrated the effectiveness of the lectin p...Continue Reading

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Citations

Jan 1, 2021·Proceedings of the National Academy of Sciences of the United States of America·Jennyfer Tena, Carlito B Lebrilla
May 29, 2021·Mass Spectrometry Reviews·Fangxu SunRonghu Wu

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Methods Mentioned

BETA
glycosylation
enzyme-linked lectin assay
protein folding
acetylation

Software Mentioned

Glycam
MassHunter Qualitative Analysis
Imaris
STRING
ChimeraX
Byonic
Byologic

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