Coupling Aptamer‐based Protein Tagging with Metabolic Glycan Labeling for In Situ Visualization and Biological Function Study of Exosomal Protein‐Specific Glycosylation. (9th July 2021)
- Record Type:
- Journal Article
- Title:
- Coupling Aptamer‐based Protein Tagging with Metabolic Glycan Labeling for In Situ Visualization and Biological Function Study of Exosomal Protein‐Specific Glycosylation. (9th July 2021)
- Main Title:
- Coupling Aptamer‐based Protein Tagging with Metabolic Glycan Labeling for In Situ Visualization and Biological Function Study of Exosomal Protein‐Specific Glycosylation
- Authors:
- Zhu, Lin
Xu, Yuanfeng
Wei, Xinyu
Lin, Haoting
Huang, Mengjiao
Lin, Bingqian
Song, Yanling
Yang, Chaoyong - Abstract:
- Abstract: Exosomal glycoproteins play important roles in many physiological and pathological functions. Herein, we developed a dual labeling strategy based on a protein‐specific aptamer tagging and metabolic glycan labeling for visualizing glycosylation of specific proteins on exosomes. The glycosylation of exosomal PD‐L1 (exoPD‐L1) was imaged in situ using intramolecular fluorescence resonance energy transfer (FRET) between fluorescent PD‐L1 aptamers bound on exoPD‐L1 and fluorescent tags on glycans introduced via metabolic glycan labeling. This method enables in situ visualization and biological function study of exosomal protein glycosylation. Exosomal PD‐L1 glycosylation was confirmed to be required in interaction with PD‐1 and participated in inhibiting of CD8 + T cell proliferation. This is an efficient and non‐destructive method to study the presence and function of exosomal protein‐specific glycosylation in situ, which provides a powerful tool for exosomal glycoproteomics research. Abstract : A dual labeling strategy for in situ visualization of exosomal protein‐specific glycosylation based on a protein‐specific aptamer tagging and metabolic glycan labeling (ExoAp‐MGL) was used to study the presence and function of exosomal protein‐specific glycosylation. Exosomal PD‐L1 glycosylation is required for the interaction of exoPD‐L1/PD‐1 and inhibition of CD8 + T cell proliferation.
- Is Part Of:
- Angewandte Chemie. Volume 133:Number 33(2021)
- Journal:
- Angewandte Chemie
- Issue:
- Volume 133:Number 33(2021)
- Issue Display:
- Volume 133, Issue 33 (2021)
- Year:
- 2021
- Volume:
- 133
- Issue:
- 33
- Issue Sort Value:
- 2021-0133-0033-0000
- Page Start:
- 18259
- Page End:
- 18263
- Publication Date:
- 2021-07-09
- Subjects:
- aptamers -- exosomes -- glycosylation -- metabolic glycan labeling -- PD-L1
Chemistry -- Periodicals
540 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/ange.202103696 ↗
- Languages:
- English
- ISSNs:
- 0044-8249
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0902.000000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 23867.xml