Glycan microarray analysis of P-type lectins reveals distinct phosphomannose glycan recognition

Xuezheng Song, Yi Lasanajak, Linda J. Olson, Marielle Boonen, Nancy M. Dahms, Stuart Kornfeld, Richard D. Cummings, David F. Smith

Research output: Contribution to journalArticlepeer-review

58 Scopus citations


The specificity of the cation-independent and -dependent mannose 6-phosphate receptors (CI-MPR and CD-MPR) for high mannose-type N-glycans of defined structure containing zero, one, or two Man-P-GlcNAc phosphodiester or Man-6-P phosphomonoester residues was determined by analysis on a phosphorylated glycan microarray. Amine-activated glycans were covalently printed on N-hydroxysuccinimide-activated glass slides and interrogated with different concentrations of recombinant CD-MPR or soluble CI-MPR. Neither receptor bound to non-phosphorylated glycans. The CD-MPR bound weakly or undetectably to the phosphodiester derivatives, but strongly to the phosphomonoester-containing glycans with the exception of a single Man7GlcNAc2-R isomer that contained a single Man-6-P residue. By contrast, the CI-MPR bound with high affinity to glycans containing either phospho-mono- or -diesters although, like the CD-MPR, it differentially recognized isomers of phosphorylated Man7GlcNAc2-R. This differential recognition of phosphorylated glycans by the CI- and CD-MPRs has implications for understanding the biosynthesis and targeting of lysosomal hydrolases.

Original languageEnglish
Pages (from-to)35201-35214
Number of pages14
JournalJournal of Biological Chemistry
Issue number50
StatePublished - Dec 11 2009


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