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1.
Molecules ; 18(5): 5792-803, 2013 May 17.
Article in English | MEDLINE | ID: mdl-23685936

ABSTRACT

Rhizobium tropici is a Gram-negative bacterium that induces nodules and fixed atmospheric nitrogen in symbiotic association with Phaseolus vulgaris (common bean) and some other leguminous species. Lectins are proteins that specifically bind to carbohydrates and, consequently, modulate different biological functions. In this study, the d-glucose/ d-mannose-binding lectins (from seeds of Dioclea megacarpa, D. rostrata and D. violacea) and D-galactose-binding lectins (from seeds of Bauhinia variegata, Erythina velutina and Vatairea macrocarpa) were purified using chromatographic techniques and evaluated for their effect on the growth of R. tropici CIAT899. All lectins were assayed with a satisfactory degree of purity according to SDS-PAGE analysis, and stimulated bacterial growth; in particular, the Dioclea rostrata lectin was the most active among all tested proteins. As confirmed in the present study, both d-galactose- and d-glucose/d-mannose-binding lectins purified from the seeds of leguminous plants may be powerful biotechnological tools to stimulate the growth of R. tropici CIAT99, thus improving symbiotic interaction between rhizobia and common bean and, hence, the production of this field crop.


Subject(s)
Fabaceae/chemistry , Plant Lectins , Rhizobium tropici/growth & development , Seeds/chemistry , Plant Lectins/chemistry , Plant Lectins/isolation & purification , Plant Lectins/pharmacology
2.
Molecules ; 17(5): 5244-54, 2012 May 07.
Article in English | MEDLINE | ID: mdl-22565477

ABSTRACT

To study the interactions between a Rhizobium tropici strain and lectins isolated from the seeds of Canavalia ensiformis (ConA) and Canavalia brasiliensis (ConBr), a lectin fluorescence assay was performed. In addition, an experiment was designed to evaluate the effect of the two lectins on bacterial growth. Both lectins were found to bind to R. tropici cells, but the interactions were inhibited by D-mannose. Interestingly, only ConBr stimulated bacterial growth in proportion to the concentrations used (15.6-500 µg/mL), and the bacterial growth stimulation was inhibited by D-mannose as well. Structure/Function analyses by bioinformatics were carried out to evaluate the volume and carbohydrate recognition domain (CRD) configuration of ConA and ConBr. The difference of spatial arrangement and volume of CRD may indicate the variation between biological activities of both lectins. The results suggest that ConBr could be a promising tool for studies focusing on the interactions between rhizobia and host plants.


Subject(s)
Canavalia/chemistry , Plant Lectins/pharmacology , Rhizobium tropici/drug effects , Seeds/chemistry , Biological Assay , Dose-Response Relationship, Drug , Fluorescein-5-isothiocyanate , Fluorescent Dyes , Mannose/pharmacology , Models, Molecular , Nitrogen Fixation/physiology , Plant Lectins/isolation & purification , Plant Lectins/metabolism , Protein Binding/drug effects , Protein Structure, Tertiary , Rhizobium tropici/physiology , Spectrometry, Fluorescence , Structure-Activity Relationship
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