Carbohydrate specificity of the receptor sites of mistletoe toxic lectin-I

Albert M. Wu*, Lee Kian Chin, Hartmut Franz, Uwe Pfüller, Anthony Herp

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

36 Scopus citations


The carbohydrate specificity of mistletoe toxic lectin-I (ML-I) was studied by haemagglutination-inhibition assay. The results indicated that ML-I has a broad range of affinity for Gal, α, β linked sequences. The galabiose (C, Galα1→4Gal) sequence, a receptor of the uropathogenic E. coli ligand, was one of the best disaccharide inhibitors tested. The lectin also exhibits affinity for Lac(Galβ1→4Glc), T(Galβ1→3GalNAc), I/II(Galβ1→3/4GlcNAc) and B(Galα1→3Gal) sequences. Galα1→4Gal and Galβ1→4Glc are frequently occurring sequences of many glycosphingolipids located at the mammalian cell membranes, such as intestinal and red blood cell membranes, for ligand binding and toxin attachment. This finding provides important information concerning the possible mechanism of intoxication of cells by the mistletoe preparation.

Original languageEnglish
Pages (from-to)232-234
Number of pages3
JournalBiochimica et Biophysica Acta - General Subjects
Issue number2
StatePublished - 15 09 1992


  • Carbohydrate binding property
  • Carbohydrate combining site
  • Haemagglutination-inhibition assay
  • Mistletoe toxic lectin-I


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