PMID: 8464919Apr 1, 1993Paper

Carbohydrate binding activities of Bradyrhizobium japonicum: unipolar localization of the lectin BJ38 on the bacterial cell surface

Proceedings of the National Academy of Sciences of the United States of America
J T LohM Schindler

Abstract

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.

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Citations

Apr 3, 2001·Journal of Molecular Spectroscopy·K. D. SetzerR. J. Buenker
Jan 1, 1994·Biochimie·J P WisniewskiF M Delmotte
Aug 1, 1994·Trends in Microbiology·E L Kannenberg, N J Brewin
Nov 7, 2003·Applied and Environmental Microbiology·Joseph F JonesDarrell Velegol
Apr 9, 2014·Veterinary Microbiology·Said BenhamedMaría Ángeles Esteban
Jul 12, 2008·FEMS Microbiology Letters·Maarten Fauvart, Jan Michiels
Dec 20, 2005·Molecular Microbiology·Melanie L LawlerYves V Brun
Nov 1, 1993·Journal of Bacteriology·J R MaddockL Shapiro
Sep 10, 2015·Microbiology Spectrum·Cécile BerneYves V Brun
Dec 10, 2002·Science·Lucy ShapiroRichard Losick

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