Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 60, Issue 33, Pages 18111-18115Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202103696
Keywords
aptamers; exosomes; glycosylation; metabolic glycan labeling; PD-L1
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Funding
- National Natural Science Foundation of China [22022409, 21735004, 21874089, 21775128]
- Program for Changjiang Scholars and Innovative Research Team in University [IRT13036]
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The study developed a dual labeling strategy to visualize the glycosylation of specific proteins on exosomes, enabling in situ visualization and biological function study. Exosomal PD-L1 glycosylation was confirmed to be required in interaction with PD-1 and participated in inhibiting CD8(+) T cell proliferation, offering a powerful tool for exosomal glycoproteomics research.
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.
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