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Estudo da antibiose e destino da faseolina (Globulina - Phaseolus vulgaris) em larvas do caruncho Callosobruchus maculatus (Coleoptera: Chrysomelidae: Bruchinae)

Dissertação (mestrado) - Universidade Federal de Santa Catarina, Centro de Ciências Biológicas, Programa de Pós-Graduação em Bioquímica, Florianópolis, 2014. / Made available in DSpace on 2014-08-06T18:07:01Z (GMT). No. of bitstreams: 1
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Previous issue date: 2014 / Abstract : This work confirmed the high toxicity of the storage protein from the seeds of the common bean Phaseolus vulgaris (phaseolin) on the larvae of the seed beetle Callosobruchus maculatus. When incorporated into the diet of the larvae at physiological concentrations (0.5 %) larval mortality of C. maculatus increased. The main factor involved seems to be the accumulation of vesicles containing phaseolin in the enterocytes leading to the impairment of vesicular traffic. The fate of the seed storage globulins from cowpea Vigna unguiculata (vicilin) and from P. vulgaris (phaseolin) was monitored by fluorescence microscopy after cryostat microtomy. By feeding bean beetle larvae with vicilin/ FITC and phaseolin/ FITC noticed a difference in the absorptive process of globulins among the tested diets. The intestinal epithelium of larvae fed phaseolin/ FITC showed higher fluorescence than larvae fed vicilin. A membrane bound protein has been isolated from the intestinal epithelium of larval C. maculatus by using an affinity column where the vicilin was covalently mobilized to sepharose. This protein has a high homology with the a-tocopherol (vitamin E precursor) transfer protein. These data suggest that the vicilin molecule binds to receptors in the microvillar membrane and subsequently it may be absorbed inside vesicles within the epithelial cells of the larval midgut. This process may be a case of receptor-mediated endocytosis. These findings suggest a new mechanism of antibiosis, involving accumulation of vicilin variants and phaseolin in the intestinal epithelium of the C. maculatus larvae and commitment of endocytic processes. This mechanism probably involves the binding of vicilin/phaseolin protein homologous to a a-tocopherol transfer protein, thereby killing the insect by the lack of absorption of important nutrients for development,such as the vitamin E.

Identiferoai:union.ndltd.org:IBICT/oai:repositorio.ufsc.br:123456789/123357
Date January 2014
CreatorsKunz, Daniele
ContributorsUniversidade Federal de Santa Catarina, Silva, Carlos Peres
Source SetsIBICT Brazilian ETDs
LanguagePortuguese
Detected LanguageEnglish
Typeinfo:eu-repo/semantics/publishedVersion, info:eu-repo/semantics/masterThesis
Format79 p.| il., grafs.
Sourcereponame:Repositório Institucional da UFSC, instname:Universidade Federal de Santa Catarina, instacron:UFSC
Rightsinfo:eu-repo/semantics/openAccess

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