Carbohydrate binding activities of Bradyrhizobium japonicum: unipolar localization of the lectin BJ38 on the bacterial cell surface.
Carbohydrate binding activities of Bradyrhizobium japonicum: unipolar localization of the lectin BJ38 on the bacterial cell surface.
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日本慢生根瘤菌的碳水化合物结合活性：凝集素 BJ38 在细菌细胞表面的单极定位。
DOI：
10.1073/pnas.90.7.3033
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发表时间：
1993
影响因子：
11.1
通讯作者：
Schindler,M
中科院分区：
文献类型：
--
作者：
Loh,JT;Ho,SC;deFeijter,AW;Wang,JL;Schindler,M
针对慢生型日本根瘤菌凝集素BJ38制备的多克隆抗血清具有针对该蛋白的特异性。用该抗血清处理日本血吸虫细胞，然后用透射电子显微镜和常规荧光显微镜和共聚焦荧光显微镜观察，发现BJ38只在细菌的一极。BJ38呈簇状排列，与细菌外膜分离。BJ38的定位与(I)与其他日本血吸虫细胞的同型凝集，(Ii)与培养的大豆细胞系SB-1的黏附，以及(Iii)与乳糖共价衍生化的琼脂糖珠的吸附位置一致。相反，植物凝集素大豆凝集素在远离细菌附着位置的极点标记细菌。这些结果表明，BJ38的拓扑分布与该细菌凝集素在日本血吸虫与其他细胞和表面的极性结合中的作用是一致的。
A polyclonal antiserum generated against the Bradyrhizobium japonicum lectin BJ38 was characterized to be specifically directed against the protein. Treatment of B. japonicum cells with this antiserum and subsequent visualization with transmission electron microscopy and both conventional and confocal fluorescence microscopy revealed BJ38 at only one pole of the bacterium. BJ38 appeared to be organized in a tuft-like mass, separated from the bacterial outer membrane. BJ38 localization was coincident with the attachment site for (i) homotypic agglutination to other B. japonicum cells, (ii) adhesion to the cultured soybean cell line SB-1, and (iii) adsorption to Sepharose beads covalently derivatized with lactose. In contrast, the plant lectin soybean agglutinin labeled the bacteria at the pole distant from the bacterial attachment site. These results indicate that the topological distribution of BJ38 is consistent with a suggested role for this bacterial lectin in the polar binding of B. japonicum to other cells and surfaces.