Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc

Chin Fen Teo, Sampat Ingale, Margreet A Wolfert, Galal A Elsayed, Laszlo G Nöt, John C Chatham, Lance Wells, Geert-Jan Boons

Research output: Contribution to journalArticleAcademicpeer-review


Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization. We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology. Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins. A substantial number of the glycoproteins were enriched by only one of the antibodies. This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants. The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.

Original languageEnglish
Pages (from-to)338-43
Number of pages6
JournalNature Chemical Biology
Issue number5
Publication statusPublished - 2010
Externally publishedYes


  • Acetylglucosamine
  • Antibodies, Monoclonal
  • Enzyme-Linked Immunosorbent Assay
  • Glycopeptides
  • Immunoprecipitation


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