The visualization of glycosylation
states of specific
proteins in vivo is of great importance for uncovering
their roles in disease development. However, the ubiquity of glycosylation
makes probing the glycans on a certain protein as difficult as looking
for a needle in a haystack. Herein, we demonstrate a proximity-induced
hybridization chain reaction (HCR) strategy for amplified visualization
of protein-specific glycosylation. The strategy relies on designing
two kinds of DNA probes, glycan conversion probes and protein recognition
probes, which are attached to glycans and target proteins, respectively.
Upon sequential binding to the targets, the proximity-induced hybridization
between two probes occurs, which leads to the structure-switching
of protein recognition probes, followed by triggering of HCR assembly.
This strategy has been used to visualize tyrosine-protein kinase 7-specific
sialic acid in living CEM cells and zebrafish and to monitor
its variation during drug treatment. It provides a potential tool
for investigating protein-specific glycosylation and researching
the relation between dynamic glycans state and disease process.
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