Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: quantitative analysis by frontal affinity chromatography

Glycobiology. 2006 Jan;16(1):46-53. doi: 10.1093/glycob/cwj038. Epub 2005 Sep 21.


Jacalin, a lectin from the jackfruit Artocarpus integrifolia, has been known as a valuable tool for specific capturing of O-glycoproteins such as mucins and IgA1. Though its sugar-binding preference for T/Tn-antigens is well established, its detailed specificity has not been elucidated. In this study, we prepared a series of mucin-type glycopeptides using human glycosyltransferases, that is, ST6GalNAc1, Core1Gal-T1 and -T2, beta3Gn-T6, and Core2GnT1, and investigated their binding to immobilized Jacalin by frontal affinity chromatography (FAC). As a result, consistent with the previous observation, Jacalin showed high affinity for T-antigen (Core1) and Tn-antigen (alpha N-acetylgalactosamine)-attached peptides. Furthermore, we here show as novel findings that (1) Jacalin also showed significant affinity for Core3 and sialyl-T (ST)-attached peptides, but (2) Jacalin could not bind to Core2, Core6, and sialyl-Tn (STn)-attached peptides. The results were also confirmed by FAC using p-nitrophenyl (pNP)-derivatized saccharides. In conclusion, Jacalin binds to a GalNAcalpha1-peptide, in which C6-OH of alphaGalNAc is free (i.e., Core1, Tn, Core3, and ST), whereas it cannot recognize a GalNAcalpha1-peptide with a substitution at the C6 position (i.e., Core2, Core6, and STn). These findings provide useful information when applying jacalin for functional analysis of mucin-type glycoproteins and glycopeptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Tumor-Associated, Carbohydrate / chemistry*
  • Antigens, Tumor-Associated, Carbohydrate / metabolism
  • Chromatography, Affinity
  • Glucosyltransferases / chemistry*
  • Humans
  • Mucins / chemistry*
  • Mucins / metabolism
  • Oligopeptides / chemistry*
  • Oligopeptides / metabolism
  • Plant Lectins / chemistry*
  • Plant Lectins / metabolism
  • Protein Binding
  • Substrate Specificity


  • Antigens, Tumor-Associated, Carbohydrate
  • Mucins
  • Oligopeptides
  • Plant Lectins
  • Tn antigen
  • jacalin
  • Glucosyltransferases