Cell-surface tethered promiscuous biotinylators enable comparative small-scale surface proteomic analysis of human extracellular vesicles and cells
elifesciences.org
we employed horseradish peroxidase (HRP) fused to the glycan-binding domain of wheat germ agglutinin (WGA-HRP) cancer-derived EVs are unique from the EVs derived from healthy surrounding tissues However, strategies for the unbiased profiling of small EV membrane proteomes remain limited. Isolation o
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- we employed horseradish peroxidase (HRP) fused to the glycan-binding domain of wheat germ agglutinin (WGA-HRP)
- cancer-derived EVs are unique from the EVs derived from healthy surrounding tissues
- However, strategies for the unbiased profiling of small EV membrane proteomes remain limited. Isolation of high-quality, enriched small EV populations is challenging, requiring numerous centrifugation steps and a final sucrose gradient isolation, precluding the use of current labeling methods for membrane proteome characterization
- with or without oncogenic Myc induction
- ether there was a bias toward Uniprot annotated ‘Glycoprotein’ versus ‘Non-Glycoprotein’ surface proteins identified across the WGA-HRP, APEX2-DNA, APEX2, and HRP labeling methods.
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