O-glycosylation sites identified from mucin core-1 type glycopeptides from human serum

Zsuzsanna Darula, Farkas Sarnyai, Katalin F. Medzihradszky

Research output: Article

16 Citations (Scopus)

Abstract

In this work O-linked glycopeptides bearing mucin core-1 type structures were enriched from human serum. Since about 70 % of the O-glycans in human serum bind to the plant lectin Jacalin, we tested a previously successful protocol that combined Jacalin affinity enrichment on the protein- and peptide-level with ERLIC chromatography as a further enrichment step in between, to eliminate the high background of unmodified peptides. In parallel, we developed a simpler and significantly faster new workflow that used two lectins sequentially: wheat germ agglutinin and then Jacalin. The first lectin provides general glycopeptide enrichment, while the second specifically enriches O-linked glycopeptides with Galβ1-3GalNAcα structures. Mass spectrometric analysis of enriched samples showed that the new sample preparation method is more selective and sensitive than the former. Altogether, 52 unique glycosylation sites in 20 proteins were identified in this study.

Original languageEnglish
Pages (from-to)435-445
Number of pages11
JournalGlycoconjugate Journal
Volume33
Issue number3
DOIs
Publication statusPublished - jún. 1 2016

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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