Sugar-lectin interactions: how does wheat-germ agglutinin bind sialoglycoconjugates?

Eur J Biochem. 1980 Feb;104(1):147-53. doi: 10.1111/j.1432-1033.1980.tb04410.x.


The specific binding of N-acetylneuraminic acid to wheat-germ agglutinin is based on configuration similarities between N-acetylneuraminic acid and N-acetylglucosamine. The N-acetamido group and an adjacent hydroxyl group, both in an equatorial position are shown to be the main determinants. The N-acetylneuraminic acid--wheat-germ agglutinin interaction is increased by the removal of the last two carbons C8 and C9. The interaction between wheat-germ agglutinin and glycoconjugates containing N-acetylneuraminic acid is shown to be dependent on a charge effect and on an avidity effect. Succinylated wheat-germ agglutinin which is negatively charged at physiological pH, in contrast with wheat-germ agglutinin which is positively charged, does not bind cell surface glycoconjugates containing N-acetylneuraminic acid but does bind cell surface glycoconjugates containing N-acetylglucosamine. The use of wheat-germ agglutinin and of succinylated wheat-germ agglutinin leads to the determination of the number of cell surface receptors containing N-acetylneuraminic acid.

MeSH terms

  • Acetylglucosamine*
  • Animals
  • Carbohydrate Conformation
  • Carbohydrates*
  • Cell Line
  • Chemical Phenomena
  • Chemistry
  • Cricetinae
  • Gangliosides
  • Glucosamine* / analogs & derivatives
  • Kidney
  • Kinetics
  • Lectins*
  • Neuraminidase
  • Sialic Acids*
  • Structure-Activity Relationship
  • Wheat Germ Agglutinins


  • Carbohydrates
  • Gangliosides
  • Lectins
  • Sialic Acids
  • Wheat Germ Agglutinins
  • Neuraminidase
  • Glucosamine
  • Acetylglucosamine