TWO-DIMENSIONAL ELECTROPHORESIS-BASED PROTEOMIC ANALYSIS OF PHASEOLUS VULGARIS IN RESPONSE TO COLLETOTRICHUM LINDEMUTHIANUM

Brazil is the largest producer of the common bean (Phaseolus vulgaris L.), a staple food for a large proportion of the Brazilian population and its main protein source. Bean anthracnose is a common and broadly distributed bean disease and can cause yield losses of up to 100%. Alterations in the prot...

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Bibliographic Details
Published in:Journal of plant pathology 2015-07, Vol.97 (2), p.249-257
Main Authors: Borges, L.L., Santana, F.A., Castro, I.S.L., Arruda, K.M.A., Ramos, H.J.O., Barros, E.G.
Format: Article
Language:English
Subjects:
Beans
Chalconoids
Gels
Inoculation
Peptide elongation factors
Phytopathology
Plant interaction
Plants
Proteomes
Proteomics
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Summary:Brazil is the largest producer of the common bean (Phaseolus vulgaris L.), a staple food for a large proportion of the Brazilian population and its main protein source. Bean anthracnose is a common and broadly distributed bean disease and can cause yield losses of up to 100%. Alterations in the proteome of common bean leaves as a response to challenge by Colletotrichum lindemuthianum were analyzed using two-dimensional gel electrophoresis and mass spectrometry. The cultivar AND 277 was inoculated with an incompatible race of C. lindemuthianum. In comparison with non-inoculated plants, we observed 34 proteins differentially accumulated in leaves collected 12, 24, and 48 h post inoculation. The protein spots obtained from 2DE gels were then analyzed by MALDITOF/TOF mass spectrometry. Seventeen proteins were identified by MS/MS fragmentation. Most of them corresponded to enzymes belonging to photosynthesis and carbon metabolism, antioxidant systems, genetic information processing, defense and stress response, chaperones and folding catalysts, and phenylpropanoid or flavonoid biosynthesis. Our findings indicate that these proteins are related to the common bean response to C. lindemuthianum.
ISSN:1125-4653
2239-7264
DOI:10.4454/JPP.V97I2.026