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Cell Surface Interactions of Rhizobium Bacteroids and Other Bacterial Strains with Symbiosomal and Peribacteroid Membrane Components from Pea Nodules

February 2004 , Volume 17 , Number  2
Pages  216 - 223

Luis Bolaños , 1 Miguel Redondo-Nieto , 1 Rafael Rivilla , 1 Nicholas J. Brewin , 2 and Ildefonso Bonilla 1

1Departamento de Biología, Universidad Autónoma de Madrid, 28049-Madrid, Spain; 2Department of Genetics, John Innes Centre, Norwich Research Park, Colney Lane, Norwich NR4 7UH, U.K.

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Accepted 12 October 2003.

Samples of Rhizobium bacteroids isolated from pea nodule symbiosomes reacted positively with a monoclonal antibody recognizing N-linked glycan epitopes on plant glycoproteins associated with the peribacteroid membrane and peribacteroid fluid. An antiserum recognizing the symbiosomal lectin-like glycoprotein PsNLEC-1 also reacted positively. Samples of isolated bacteroids also reacted with an antibody recognizing a glycolipid component of the peribacteroid membrane and plasma membrane. Bacterial cells derived from free-living cultures then were immobilized on nitrocellulose sheets and tested for their ability to associate with components of plant extracts derived from nodule fractionation. A positive antibody-staining reaction indicated that both PsNLEC-1 and membrane glycolipid had become associated with the bacterial surface. A range of rhizobial strains with mutants affecting cell surface polysaccharides all showed similar interactions with PsNLEC-1 and associated plant membranes, with the exception of strain B659 (a deep-rough lipopolysaccharide mutant of Rhizobium leguminosarum). However, the presence of a capsule of extracellular polysaccharide apparently prevented interactions between rhizobial cells and these plant components. The importance of a close association between peribacteroid membranes, PsNLEC-1, and the bacterial surface is discussed in the context of symbiosome development.

© 2004 The American Phytopathological Society