Maenuma Keisuke, Yim Mijung, Komatsu Kunimitsu, Hoshino Mayumi, Takahashi Yoriko, Bovin Nicolai, Irimura Tatsuro
Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Proteomics. 2008 Aug;8(16):3274-83. doi: 10.1002/pmic.200800037.
Thirty-five variant lectins were prepared by mutations of two amino acids within the carbohydrate-recognition domain of Maackia amurensis hemagglutinin (MAH). Each lectin showed unique carbohydrate specificity according to their bindings to soluble polyacrylamide with various mono- and oligosaccharides and to glycophorin A. The relative intensity of the bindings of carcinoma, myeloid, fibroblastic, and melanoma cells to immobilized MAH variant lectins was examined. Each cell line showed distinct profiles regarding the number of cells bound to wild-type and 35 MAH variants and the differences and the similarities in these binding profiles were quantitatively documented by the cluster analysis. The cell lines were classified into several groups and these groups surprisingly corresponded to the lineage of the cells. These results indicated that a library of mutated MAH is useful as a tool for the profiling of various cells based on the variations of the surface glycans.
通过对山槐血凝素（MAH）碳水化合物识别域内的两个氨基酸进行突变，制备了35种变体凝集素。根据它们与带有各种单糖和寡糖的可溶性聚丙烯酰胺以及血型糖蛋白A的结合情况，每种凝集素都表现出独特的碳水化合物特异性。检测了癌细胞、髓样细胞、成纤维细胞和黑色素瘤细胞与固定化MAH变体凝集素结合的相对强度。每个细胞系在与野生型和35种MAH变体结合的细胞数量方面表现出不同的特征，并且通过聚类分析定量记录了这些结合特征中的差异和相似性。细胞系被分为几个组，令人惊讶的是，这些组与细胞谱系相对应。这些结果表明，突变MAH文库可作为一种基于表面聚糖变化对各种细胞进行分析的工具。
