Binding specificities of the lectins PNA, WGA and UEA I to polyvinylchloride‐adsorbed glycosphingolipids

FEBS Letters

Fredman, Pam¹  Molin, Kent¹  Svennerholm, Lars¹ 

[1] Department of Psychiatry and Neurochemistry, University of Gothenburg, St. Jörgen's Hospital, S-422 03 Hisings Backa, Sweden

关键词: Lectin;    Ganglioside;    Glycosphingolipid;    ELISA;    PNA;    peanut agglutinin;    WGA;    wheat germ agglutinin;    UEA I;    Ulex europeus agglutinin I. Ganglioside nomenclature according to Svennerholm [1.] Fuc-GM1 and Fuc-nLA1 are fucosylated GM1 (IV2Fuc;    II3NeuAc-GgOse4Cer) and nLA1 (III3FucnLcOse4Cer);    respectively. 3'-nLM1 and 6'-nLM1 are shorthand designations for IV3NeuAc-nLcOse4Cer and IV6NeuAc-nLcOse4Cer;    respectively. Lea is the Lewisa blood group defining antigen;    III4Fuc-LcOse4Cer (see also table 1);   

DOI  :  10.1016/0014-5793(86)80864-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Le^a glycolipid which has an α 1-4 linked fucose but not for the glycolipids with αl-3 or α 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.

【 授权许可】

Unknown