title: Purification and applications of a lectin from the mushroom Gymnopilus spectabilis.
abstract: A lectin was isolated from fruiting bodies of the mushroom Gymnopilus spectabilis (GSL) by ionic exchange chromatography. The lectin agglutinates mouse red cells exhibiting broad specificity towards several monosaccharides including the N-acetylneuraminic acid. Agglutination was also inhibited by the glycoproteins: fetuin, lactoferrin, and recombinant erythropoietin. GSL is a glycoprotein possessing 16 % of carbohydrates; the SDS-PAGE showed two bands with molecular mass of 52.1 and 64.4 kDa. Isoelectric focusing displayed microheterogeneity, with two bands at pIs 5.1 and 5.3. The lectin was stable between pH 2 and pH 8 while at pH 10, the agglutination decayed to 50 % of initial activity. Incubation at 40 and 80 °C led to 50 and 100 % loss in activity of the lectin, respectively. Synthesized GSL-Sepharose interacts with serum pregnant mare gonadotropin, and at least two subpopulations of this glycoprotein were separated. There was no interaction between transferrin and soluble GSL while a partial recognition was achieved with GSL-Sepharose. The terminal sialic acid seems to play an active role in modifying the interaction with GSL, depending if the lectin is in a soluble or immobilized form. The purified lectin inhibited in vitro the growth of Staphylococcus aureus and Aspergillus niger.
authors: Cátedra de Microbiología, DepBio, Facultad de Química, Montevideo, Uruguay.
authors: Silvana
authors: S
authors: Alborés
authors: Paola
authors: P
authors: Mora
authors: María José
authors: MJ
authors: Bustamante
authors: María Pía
authors: MP
authors: Cerdeiras
authors: Laura
authors: L
authors: Franco Fraguas
mesh_terms: D000363:Agaricales / Q000378:metabolism*; D001487:Basidiomycota / Q000378:metabolism; D048690:Fruiting Bodies, Fungal / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D037102:Lectins / Q000378:metabolism*
chemical_list: D006023:Glycoproteins; D037102:Lectins