Crystal Structure of the Marasmius Oreades Mushroom Lectin in Complex with a Xenotransplantation Epitope

MOA, a lectin from the mushroom Marasmius oreades, is one of the few reagents that specifically agglutinate blood group B erythrocytes. Further, it is the only lectin known to have exclusive specificity for Galα(1,3)Gal-containing sugar epitopes, which are antigens that pose a severe barrier to anim...

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Veröffentlicht in:Journal of molecular biology 2007-06, Vol.369 (3), p.710-721
Hauptverfasser: Grahn, Elin, Askarieh, Glareh, Holmner, Åsa, Tateno, Hiroaki, Winter, Harry C., Goldstein, Irwin J., Krengel, Ute
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Sprache:eng
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Zusammenfassung:MOA, a lectin from the mushroom Marasmius oreades, is one of the few reagents that specifically agglutinate blood group B erythrocytes. Further, it is the only lectin known to have exclusive specificity for Galα(1,3)Gal-containing sugar epitopes, which are antigens that pose a severe barrier to animal-to-human organ transplantation. We describe here the structure of MOA at 2.4 Å resolution, in complex with the linear trisaccharide Galα(1,3)Galβ(1,4)GlcNAc. The structure is dimeric, with two distinct domains per protomer: the N-terminal lectin module adopts a ricinB/β-trefoil fold and contains three putative carbohydrate-binding sites, while the C-terminal domain serves as a dimerization interface. This latter domain, which has an unknown function, reveals a novel fold with intriguing conservation of an active site cleft. A number of indications suggest that MOA may have an enzymatic function in addition to the sugar-binding properties.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2007.03.016