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Due to the scarcity of strategies to evaluate the multiple subtype monosaccharides in one specific protein simultaneously within a single assay, understanding the glycosylation mechanisms and revealing their roles in disease development become extremely challenging. Herein, a strategy of proximity DNAzyme-activated fluorescence imaging of multiplex saccharides in a protein on the cell surface via bio-orthogonal chemistry is reported. The multichannel proximity DNAzyme-activated fluorescence recovery enabled the highly selective and effective imaging analysis of multiplexed protein-specific glycosylation in situ and has been demonstrated. This strategy is successfully applied to visualize the sialylation and fucosylation in four specific proteins on different cell lines and evaluate the variations of protein-specific glycosylation in response to the alterations of the cellular physiological status. More importantly, the quantitative tracking of the terminal sialyation and fucosylation changes at the single-protein level is realized by assigning the target protein as the native reference, which has the potential to be a versatile platform for glycobiology research and clinical diagnosis.
Li et al. (Thu,) studied this question.