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.