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- Title
Cell-specific bioorthogonal tagging of glycoproteins.
- Authors
Cioce, Anna; Calle, Beatriz; Rizou, Tatiana; Lowery, Sarah C.; Bridgeman, Victoria L.; Mahoney, Keira E.; Marchesi, Andrea; Bineva-Todd, Ganka; Flynn, Helen; Li, Zhen; Tastan, Omur Y.; Roustan, Chloe; Soro-Barrio, Pablo; Rafiee, Mahmoud-Reza; Garza-Garcia, Acely; Antonopoulos, Aristotelis; Wood, Thomas M.; Keenan, Tessa; Both, Peter; Huang, Kun
- Abstract
Altered glycoprotein expression is an undisputed corollary of cancer development. Understanding these alterations is paramount but hampered by limitations underlying cellular model systems. For instance, the intricate interactions between tumour and host cannot be adequately recapitulated in monoculture of tumour-derived cell lines. More complex co-culture models usually rely on sorting procedures for proteome analyses and rarely capture the details of protein glycosylation. Here, we report a strategy termed Bio-Orthogonal Cell line-specific Tagging of Glycoproteins (BOCTAG). Cells are equipped by transfection with an artificial biosynthetic pathway that transforms bioorthogonally tagged sugars into the corresponding nucleotide-sugars. Only transfected cells incorporate bioorthogonal tags into glycoproteins in the presence of non-transfected cells. We employ BOCTAG as an imaging technique and to annotate cell-specific glycosylation sites in mass spectrometry-glycoproteomics. We demonstrate application in co-culture and mouse models, allowing for profiling of the glycoproteome as an important modulator of cellular function. Changes in glycoprotein expression are correlates of disease, but secreted glycoproteins cannot be accurately traced to their cell line of origin. Here, the authors develop a strategy to chemically tag and profile glycoproteins in a cell line-specific manner in co-culture systems and in vivo.
- Subjects
GLYCOPROTEINS; PROTEOMICS; CELL physiology; CELL lines; CARCINOGENESIS
- Publication
Nature Communications, 2022, Vol 13, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-022-33854-0