Purification of the major outer membrane protein of Azospirillum brasilense, its affinity to plant roots, and its involvement in cell aggregation

The major outer membrane protein (MOMP) of the nitrogen-fixing rhizobacterium Azospirillum brasilense strain Cd was purified and isolated by gel filtration, and antiserum against this protein was obtained. A screening of the binding of outer membrane proteins (OMPs) of A. brasilense to membrane-immo...

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Published in:	Molecular plant-microbe interactions Vol. 14; no. 4; pp. 555 - 561
Main Authors:	BURDMAN, Saul, DULGUEROVA, Gabriella, OKON, Yaacov, JURKEVITCH, Edouard
Format:	Journal Article
Language:	English
Published:	St Paul, MN APS Press 01-04-2001 The American Phytopathological Society
Subjects:	Azospirillum brasilense Azospirillum brasilense - metabolism Bacterial Outer Membrane Proteins - isolation & purification Bacterial Outer Membrane Proteins - metabolism Bacterial Outer Membrane Proteins - physiology Bacteriology Biological and medical sciences Cell Aggregation - physiology Electrophoresis, Polyacrylamide Gel flocculation Fundamental and applied biological sciences. Psychology Genetics Immunoglobulin Fab Fragments - metabolism major outer membrane protein Microbiology Plant Roots - cytology Plant Roots - metabolism Plant Roots - microbiology root attachment Monocotyledones Membrane protein Spirillales Root Vegetal microorganism relation Spirillaceae Azospirillum brasilense External membrane Adhesion Gramineae Angiospermae Bacteria Cereal Plant growth promoting rhizobacteria Spermatophyta
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Summary:	The major outer membrane protein (MOMP) of the nitrogen-fixing rhizobacterium Azospirillum brasilense strain Cd was purified and isolated by gel filtration, and antiserum against this protein was obtained. A screening of the binding of outer membrane proteins (OMPs) of A. brasilense to membrane-immobilized root extracts of various plant species revealed different affinities for the MOMP, with a stronger adhesion to extracts of cereals in comparison with legumes and tomatoes. Moreover, this protein was shown to bind to roots of different cereal seedlings in an in vitro adhesion assay. Incubation of A. brasilense cells with MOMP-antiserum led to fast agglutination, indicating that the MOMP is a surface-exposed protein. Cells incubated with Fab fragments obtained from purified MOMP-antiserum immunoglobulin G exhibited significant inhibition of bacterial aggregation as compared with controls. Bacteria preincubated with Fab fragments showed weaker adhesion to corn roots in comparison to controls without Fab fragments. These findings suggest that the A. brasilense MOMP acts as an adhesin involved in root adsorption and cell aggregation of this bacterium.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0894-0282 1943-7706
DOI:	10.1094/MPMI.2001.14.4.555