CARBOHYDRATE BINDING ACTIVITIES OF BRADYRHIZOBIUM-JAPONICUM - UNIPOLAR LOCALIZATION OF THE LECTIN BJ38 ON THE BACTERIAL-CELL SURFACE

被引：34

作者：

LOH, JT ^{[1
]}

HO, SC ^{[1
]}

DEFEIJTER, AW ^{[1
]}

WANG, JL ^{[1
]}

SCHINDLER, M ^{[1
]}

机构：

[1] MERIDIAN INSTRUMENTS INC,OKEMOS,MI 48864

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 07期

关键词：

SYMBIOSIS; BACTERIAL ADHESION; CONFOCAL FLUORESCENCE MICROSCOPY;

D O I：

10.1073/pnas.90.7.3033

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：3033 / 3037

页数：5

共 29 条

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