Binding specificities of the lectins PNA, WGA and UEA I to polyvinylchloride-adsorbed glycosphingolipids.
The binding specificities of the lectins PNA (peanut agglutinin), WGA (wheat germ agglutinin), and UEA I (Ulex europeus agglutinin I) against glycosphingolipids were investigated using an enzyme-linked immunosorbent assay (ELISA), utilizing the biotin-avidin system for detection of bound lectin. PNA showed the highest affinity to GA1, but also bound, though less strongly, to GM1 and GD1b. WGA bound to 3'-nLM1 and 6'-nLM1, the former twice as strongly as the latter, but not to any sialic acid containing glycolipid of the gangliotetraose series. UEA I showed a high affinity for the Lea glycolipid which has an alpha 1-4 linked fucose but not for the glycolipids with alpha 1-3 or alpha 1-2 linked fucose. Interestingly, 3'-nLM1 and nLA1, glycolipids lacking fucose, also bound UEA I. The results show that lectins should be used with caution for establishing terminal sugar sequences in glycosphingolipids.
D004797:Enzyme-Linked Immunosorbent Assay; D006028:Glycosphingolipids / Q000032:analysis*; D037102:Lectins; D019887:Peanut Agglutinin; D037121:Plant Lectins; D011143:Polyvinyl Chloride; D011975:Receptors, Mitogen / Q000032:analysis*; D014909:Wheat Germ Agglutinins
D006028:Glycosphingolipids; D037102:Lectins; D019887:Peanut Agglutinin; D037121:Plant Lectins; D011975:Receptors, Mitogen; C036850:Ulex europaeus lectins; D014909:Wheat Germ Agglutinins; D011143:Polyvinyl Chloride