Zenteno E, Vázquez L, Chávez R, Córdoba F, Wieruszeski J M, Montreuil J, Debray H
Laboratorio Biología Experimental, Centro de Investigaciones Biológicas J. Félix Frías, Universidad Autónoma del Estado de Morelos, Cuernavaca, México.
Glycoconj J. 1995 Oct;12(5):699-706. doi: 10.1007/BF00731267.
Sugar specificity of the Machaerocereus eruca isolectins, MeAI and MeAII, has been determined by comparing the capacity of glycans with well defined structures to inhibit their haemagglutinating activity. Both are galactose-specific isolectins with high affinity for O-glycans. However, the two M. eruca isolectins recognize different oligosaccharidic sequences belonging to O-glycosidically linked glycans from porcine stomach mucin. The minimal structure recognized by MeAI on the porcine mucin glycans is the O-glycan core Gal beta 1,3GalNAc-ol, whereas MeAII has a more extended site and interacts with a biantennary O-glycan possessing the terminal trisaccharide Fuc alpha 1,2 (GalNAc alpha 1,3) Gal beta 1,4.
通过比较具有明确结构的聚糖抑制其血凝活性的能力,已确定了多刺仙人柱(Machaerocereus eruca)同工凝集素MeAI和MeAII的糖特异性。二者均为对半乳糖具有特异性的同工凝集素,对O-聚糖具有高亲和力。然而,这两种多刺仙人柱同工凝集素识别猪胃粘蛋白中属于O-糖苷键连接聚糖的不同寡糖序列。MeAI在猪粘蛋白聚糖上识别的最小结构是O-聚糖核心Galβ1,3GalNAc-ol,而MeAII具有更广泛的结合位点,并与具有末端三糖Fucα1,2(GalNAcα1,3)Galβ1,4的双天线O-聚糖相互作用。