Premium
Comparison of the binding properties of the mushroom Marasmius oreades lectin and Griffonia simplicifolia I‐B 4 isolectin to αgalactosyl carbohydrate antigens in the surface phase
Author(s) -
Kirkeby Svend,
Winter Harry C.,
Goldstein Irwin J.
Publication year - 2004
Publication title -
xenotransplantation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.052
H-Index - 61
eISSN - 1399-3089
pISSN - 0908-665X
DOI - 10.1111/j.1399-3089.2004.00108.x
Subject(s) - griffonia simplicifolia , lectin , mushroom , chemistry , biology , biochemistry , food science
The binding of two α ‐galactophilic lectins, Marasmius oreades agglutinin (MOA), and Griffonia simplicifolia I isolectin B 4 (GS I‐B 4 ) to neoglycoproteins and natural glycoproteins were compared in a surface phase assay. Neoglycoproteins carrying various α ‐galactosylated glycans and laminin from basement membrane of mouse sarcoma that contains the xenogenic Gal α 1–3Gal1–4GlcNAc epitope were immobilized in microtiter plate wells and lectin binding determined with an enzyme‐linked assay. After 24 h of incubation, MOA had higher affinity for the xenogenic pentasaccharide (Gal α 1–3Gal1–4GlcNAc β 1–3Gal β 1–4Glc) than for the Gal α ‐monosaccharide. The binding properties of MOA and GS I‐B 4 to the xenogenic disaccharide (Gal α 1–3Gal β 1) were comparable while the binding of MOA to the xenogenic pentasaccharide was much stronger than the binding of GS I‐B 4 to the same epitope. Non‐xenogenic disaccharide‐coupled neoglycoproteins having galactose end groups linked α 1–2 or α 1–4 to Gal or linked α 1–3 to GalNAc bound very weakly to MOA, whereas GS I‐B 4 recognized all of these disaccharides with similarly high affinity. MOA also showed high affinity for laminin. The results indicate that the Marasmius oreades lectin has nearly the same affinities as does GS I‐B 4 for the simple xenogenic carbohydrate antigens, but MOA has greater affinity for the pentasaccharide and is far more specific in its binding preferences than the Griffonia lectin.