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. PN...

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Bibliographic Details
Published inFEBS letters Vol. 205; no. 1; pp. 51 - 55
Main Authors Molin, Kent, Fredman, Pam, Svennerholm, Lars
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 01.09.1986
Elsevier
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Summary: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.
Bibliography:ObjectType-Article-1
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ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)80864-X