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

Nat Chem Biol. 2010 May;6(5):338-43. doi: 10.1038/nchembio.338. Epub 2010 Mar 21.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / chemistry*
  • Acetylglucosamine / immunology
  • Antibodies, Monoclonal / immunology*
  • Enzyme-Linked Immunosorbent Assay
  • Glycopeptides / immunology*
  • Immunoprecipitation


  • Antibodies, Monoclonal
  • Glycopeptides
  • Acetylglucosamine

Associated data

  • PubChem-Substance/87577982
  • PubChem-Substance/87577983