Agrobacterium tumefaciens interaction with suspension-cultured tomato cells

Adherence of Agrobacterium tumefaciens to suspension-cultured tomato cells has been characterized using a quantitative binding assay. Saturable binding of radiolabeled A. tumefaciens to plant cells resulted in 100 to 300 bacteria bound per cell. Specificity of A. tumefaciens binding was also inferre...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1985-01, Vol.77 (1), p.35-42
Main Authors: Neff, N.T, Binns, A.N
Format: Article
Language:English
Subjects:
Agglutination
AGROBACTERIUM
AGROBACTERIUM TUMEFACIENS
Bacteria
Bacterial plant pathogens
BINDING SITE
Biological and medical sciences
cell interactions
CELL SUSPENSIONS
Cell walls
CELLS
CELLULE
CELULAS
Chemical suspensions
Cultured cells
Enzymes
Fundamental and applied biological sciences. Psychology
Lycopersicon esculentum
Pathology. Damages, economic importance
Phytopathology. Animal pests. Plant and forest protection
Plant cells
Plants
TOMATE
TOMATOES
Tumors
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Summary:Adherence of Agrobacterium tumefaciens to suspension-cultured tomato cells has been characterized using a quantitative binding assay. Saturable binding of radiolabeled A. tumefaciens to plant cells resulted in 100 to 300 bacteria bound per cell. Specificity of A. tumefaciens binding was also inferred from two additional results: (a) an initial incubation of plant cells with A. tumefaciens reduced subsequent binding of radiolabeled A. tumefaciens by 60% to 75%; (b) tomato cells bound less than three E. coli per cell. Protease treatment of plant cells had no effect on subsequent bacterial binding, but prior treatment of plant cells with pectinolytic enzymes increased binding 2- to 3-fold. Pectin-enriched and neutral polymer-enriched fractions were obtained from tomato cell walls. The soluble pectin-enriched fraction inhibited binding of bacteria to plant cells by 85% to 95%, whereas the neutral polymer fraction only partially inhibited binding. Preliminary characterization of the activity showed it is heat stable, partially inactivated by protease treatment, and substantially inactivated by acid hydrolysis.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.77.1.35