Deciphering structural elements of mucin glycoprotein recognition

Andrew Borgert, Jamie Heimburg-Molinaro, Xuezheng Song, Yi Lasanajak, Tongzhong Ju, Mian Liu, Pamela Thompson, Govind Ragupathi, George Barany, David F. Smith, Richard D. Cummings, David Live

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


Mucin glycoproteins present a complex structural landscape arising from the multiplicity of glycosylation patterns afforded by their numerous serine and threonine glycosylation sites, often in clusters, and with variations in respective glycans. To explore the structural complexities in such glycoconjugates, we used NMR to systematically analyze the conformational effects of glycosylation density within a cluster of sites. This allows correlation with molecular recognition through analysis of interactions between these and other glycopeptides, with antibodies, lectins, and sera, using a glycopeptide microarray. Selective antibody interactions with discrete conformational elements, reflecting aspects of the peptide and disposition of GalNAc residues, are observed. Our results help bridge the gap between conformational properties and molecular recognition of these molecules, with implications for their physiological roles. Features of the native mucin motifs impact their relative immunogenicity and are accurately encoded in the antibody binding site, with the conformational integrity being preserved in isolated glycopeptides, as reflected in the antibody binding profile to array components.

Original languageEnglish (US)
Pages (from-to)1031-1039
Number of pages9
JournalACS Chemical Biology
Issue number6
StatePublished - Jun 15 2012


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