Identification and Validation of Atypical N-Glycosylation Sites

Shisheng Sun, Hui Zhang

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

It is well-known that N-linked glycans usually attach to asparagine residues in the N-X-S/T motifs of proteins. However, accumulating evidence indicates that N-glycosylation could also possibly occur at other atypical motifs. In this study, we tried to identify atypical N-glycosylation sites using our recently developed solid-phase extraction of the N-linked Glycans And Glycosite-containing peptides (NGAG) method. Peptides with deamidation sites at asparagine residues but lacking a typical asparagine-X-serine/threonine sequons (N-X-S/T, X is any amino acid except proline) motif were identified from deglycosylated peptide data as potentially atypical glycosite-containing peptides. These atypical glycosites were verified by the presence of glycans on their intact glycopeptides and further confirmed by specific inhibition of cells with an N-linked glycosylation inhibitor, tunicamycin. From this study, two atypical N-linked glycosylation sites with N-X-C and N-X-V motifs were identified and validated from an ovarian cancer cell line (OVCAR-3).

Original languageEnglish (US)
Pages (from-to)11948-11951
Number of pages4
JournalAnalytical Chemistry
Volume87
Issue number24
DOIs
StatePublished - Dec 15 2015

ASJC Scopus subject areas

  • Analytical Chemistry

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