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J. Biol. Chem., Vol. 277, Issue 17, 14996-15001, April 26, 2002

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The Mushroom Marasmius oreades Lectin Is a Blood Group Type B Agglutinin That Recognizes the Gal1,3Gal and Gal1,3Gal1,4GlcNAc Porcine Xenotransplantation Epitopes with High Affinity^*

Harry C. Winter, Kazem Mostafapour, and Irwin J. Goldstein^§

From the Department of Biological Chemistry, University of Michigan, Medical School, Ann Arbor, Michigan 48109-0606 and the  Department of Natural Sciences, University of Michigan, Dearborn, Michigan 48128-1491

A blood group B-specific lectin from the mushroom Marasmius oreades (MOA) was investigated with respect to its molecular structure and carbohydrate binding properties. SDS-PAGE mass spectrometric analysis showed it to consist of an intact (H; 33 kDa) and truncated (L; 23 kDa) subunit in addition to a small polypeptide (P; 10 kDa). Isolation in the presence of EDTA produced only the H subunits, indicating that the latter two are formed by metalloprotease cleavage of the intact H subunit. Tryptic digestion of the H, L, and P polypeptide chains followed by mass spectral analysis supports this view. The lectin strongly precipitated blood group type B substance, was nonreactive with type A substance, and reacted weakly with type H substance. Carbohydrate binding studies reveal a high affinity for Gal1,3Gal (but not for the isomeric 1,2-, 1,4-, and 1,6-disaccharides); Gal1,3Gal1,4GlcNAc; and the type B branched trisaccharide. MOA also reacts strongly with murine laminin from the Engelbreth-Holm-Swarm sarcoma and bovine thyroglobulin, both of which contain multiple Gal1,3Gal1,4GlcNAc end groups. This linear B trisaccharide is a component of porcine tissues and organs, preventing their transplantation into humans. MOA also shares carbohydrate recognition of this trisaccharide with toxin A elaborated by Clostridium difficile.

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