Gooi H C, Picard J K, Hounsell E F, Gregoriou M, Rees A R, Feizi T
Mol Immunol. 1985 Jun;22(6):689-93. doi: 10.1016/0161-5890(85)90099-9.
The carbohydrate specificity of the monoclonal antibody EGR/G49, raised against the epidermal growth factor (EGF) receptor of A431 cells, has been investigated by assessing its interactions with glycoproteins and erythrocytes derived from individuals of known blood group ABH, Lewis and secretor types, and by inhibition of binding assays using structurally defined oligosaccharides. The results indicate that this antibody reacts with the difucosylated blood group structures ALeb and ALey: (formula; see text) This antibody differs from the previously described anti-EGF receptor antibody. TL5, which is directed at the terminal blood group A trisaccharide structure and reacts poorly with the ALeb/Ley structures. Since both antibodies were selected for their reactivities with the receptor for EGF, their specificities provide evidence for the presence of both the mono- and difucosylated blood group A structures on the receptor glycoprotein. These antibodies will be invaluable in the studies of the distribution and the roles of blood group related carbohydrate structures in the organisation and function of the EGF and other receptor systems.
针对A431细胞表皮生长因子(EGF)受体产生的单克隆抗体EGR/G49的碳水化合物特异性,已通过评估其与已知ABH血型、Lewis血型和分泌型个体来源的糖蛋白及红细胞的相互作用,以及使用结构明确的寡糖进行结合抑制试验来进行研究。结果表明,该抗体与双岩藻糖化血型结构ALeb和ALey发生反应:(分子式;见正文)此抗体不同于先前描述的抗EGF受体抗体TL5,TL5针对末端血型A三糖结构,与ALeb/Ley结构反应较弱。由于这两种抗体均因其与EGF受体的反应性而被筛选出来,它们的特异性为受体糖蛋白上存在单岩藻糖化和双岩藻糖化血型A结构提供了证据。这些抗体在研究血型相关碳水化合物结构在EGF及其他受体系统的组织和功能中的分布及作用方面将具有重要价值。