Uncovering protein glycosylation dynamics and heterogeneity using deep quantitative glycoprofiling (DQGlyco).

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Tác giả: Isabelle Becher, Amber Brauer-Nikonow, Mira Lea Burtscher, Martin Garrido-Rodriguez, Cecile Le Sueur, Clément M Potel, Mikhail M Savitski, Athanasios Typas, Michael Zimmermann

Ngôn ngữ: eng

Ký hiệu phân loại: 620.1074 Engineering mechanics and materials

Thông tin xuất bản: United States : Nature structural & molecular biology , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 49959

 Protein glycosylation regulates essential cellular processes such as signaling, adhesion and cell-cell interactions
  however, dysregulated glycosylation is associated with diseases such as cancer. Here we introduce deep quantitative glycoprofiling (DQGlyco), a robust method that integrates high-throughput sample preparation, highly sensitive detection and precise multiplexed quantification to investigate protein glycosylation dynamics at an unprecedented depth. Using DQGlyco, we profiled the mouse brain glycoproteome, identifying 177,198 unique N-glycopeptides-25 times more than previous studies. We quantified glycopeptide changes in human cells treated with a fucosylation inhibitor and characterized surface-exposed glycoforms. Furthermore, we analyzed tissue-specific glycosylation patterns in mice and demonstrated that a defined gut microbiota substantially remodels the mouse brain glycoproteome, shedding light on the link between the gut microbiome and brain protein functions. Additionally, we developed a novel strategy to evaluate glycoform solubility, offering new insights into their biophysical properties. Overall, the in-depth profiling offered by DQGlyco uncovered extensive complexity in glycosylation regulation.
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