Müthing et al. 2004

ABSTRACT: Mistletoe lectin I (ML-I) is a type II ribosome-inactivating protein, which inhibits the protein biosynthesis at the ribosomal level. ML-I is composed of a catalytically active A-chain with rRNA N-glycosidase activity and a B-chain with carbohydrate binding specificities. Using comparative solidphase binding assays along with electrospray ionization tandem mass spectrometry, ML-I was shown to preferentially bind to terminally R2-6-sialylated neolacto series gangliosides from human granulocytes. IV6 Neu5Ac-nLc4Cer, VI6 Neu5Ac-nLc6Cer, and VIII6 Neu5Ac-nLc8Cer were identified as ML-I receptors, whereas the isomeric R2-3-sialylated neolacto series gangliosides were not recognized. Only marginal binding of ML-I to terminal galactose residues of neutral glycosphingolipids with a Galâ1-4Glc or Galâ14GlcNA…