Detalhes bibliográficos
| Ano de defesa: |
2017 |
| Autor(a) principal: |
Santana, Andrea Leite Camargo
 |
| Orientador(a): |
Pereira, Maristela
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| Banca de defesa: |
Pereira, Maristela,
Baeza, Lilian Cristiane,
Parente, Juliana Alves |
| Tipo de documento: |
Dissertação
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| Tipo de acesso: |
Acesso aberto |
| Idioma: |
por |
| Instituição de defesa: |
Universidade Federal de Goiás
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| Programa de Pós-Graduação: |
Programa de Pós-graduação em Genética e Biologia Molecular
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| Departamento: |
Instituto de Ciências Biológicas - ICB (RG)
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| País: |
Brasil
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| Palavras-chave em Português: |
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| Palavras-chave em Inglês: |
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| Área do conhecimento CNPq: |
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| Link de acesso: |
http://repositorio.bc.ufg.br/tede/handle/tede/7211
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Resumo: |
Paracoccidioides fungi are the causative agents of paracoccidioidomycosis, an endemic disease in Latin America with great socioeconomic importance. Inhalation of spores, the infectious particles of the fungus, is a common way to get the infection. Its treatment is slow and generates long-term side effects making it necessary to study new metabolic pathways that can be potential targets for antifungal development. In this context, stands out the chiquimate pathway in Paracoccidioides spp., related to the production of chorismate and production of aromatic amino acids, and the chorismate synthase involved in the last stage of this pathway. The chorismate synthase from Pb18 was cloned into pGEX-4T3 vector, expressed in pLysS cells and purified on a glutathione-sepharose column. Antibodies were produced from the immunization of mice with the recombinant protein obtained and used in Western blot assay to confirm protein expression. For characterization of the enzyme, its modeling was carried out. Pull-down-GST assay was performed to identify interactions between the chorismate synthase and soluble proteins present in total protein extract of Pb18. The interactions found included proteins of different functional categories related to protein synthesis, related with metabolism of common intermediates such as folate and quinolinate or related with the availability of ATP, phosphoenolpyruvate and erythrose-4-phosphate required in the chiquimate pathway. Unexpected interactions with proteins of the cell cycle and also with regulating proteins of the cell division process were observed. |
