110 resultados para Genetic characterization
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Foi realizada a caracterização genética das cultivares de pêssego Tropical e Douradão pelo método RAPD, em comparação com 'Dourado-1', 'Tutu', 'Maravilha', 'Rubro-sol', 'Flordaprince', 'Aurora-1' e 'Talismã' do Banco Ativo de Germoplasma de Frutas de Caroço do IAC, mantido no Núcleo de Agronomia de Capão Bonito, utilizando DNA extraído de folhas jovens. Foram obtidos 31 marcadores genéticos a partir dos primers altamente polimórficos OPAD10, OPAE04, OPAE07, OPAE09, OPAE11, OPAJ04 e OPAJ06, selecionados de 96 primers avaliados. Os marcadores RAPD utilizados indicaram eficientemente o grau de parentesco entre cultivares, exceto em cultivares originadas de polinização livre. Verificou-se que, mesmo entre as cultivares irmãs como 'Tutu' e 'Talismã', encontrou-se certa distância genética (0,29), mostrando que por RAPD é possível caracterizar-se germoplasma aparentado. 'Tropical' e 'Douradão' foram bem caracterizados em relação aos parentais e demais cultivares, com as distâncias genéticas variando de 0,26 a 0,89.
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Isolates of bovine viral diarrhoea virus (BVDV) detected in serum samples of two persistently infected animals (PI) identified in a herd located in the southern state of Minas Gerais, Brazil, underwent genetic characterization trough partial nucleotide sequencing and analysis of the 5' Untranslated Region (5'UTR) of the viral genome. The isolates were characterized as belonging to genotype BVDV-1, subgenotype BVDV-1b. The results of this study suggest BVDV-1b as an agent of importance in the occurrence of bovine viral diarrhoea (BVD) in the herds of the region. Moreover, the genotypic characterization of isolates of BVDV helps to better understand the epidemiology of the disease, as the genetic variability of BVDV interferes in the serological tests and has implications for the use of vaccines, whose majority is produced only with reference strains of BVDV. Therefore, the investigation on the genetic diversity of BVDV existing in Brazil is required for the improvement of the disease prevention and control measures.
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Pós-graduação em Microbiologia - IBILCE
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Pós-graduação em Ciências Biológicas (Botânica) - IBB
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Pós-graduação em Agronomia (Horticultura) - FCA
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The recent recrudescence of Mycobacterium tuberculosis infection and the emergence of multidrug-resistant strains have created an urgent need for new therapeutics against tuberculosis. The enzymes of the shikimate pathway are attractive drug targets because this route is absent in mammals and, in M. tuberculosis, it is essential for pathogen viability. This pathway leads to the biosynthesis of aromatic compounds, including aromatic amino acids, and it is found in plants, fungi, bacteria, and apicomplexan parasites. The aroB-encoded enzyme dehydroquinate synthase is the second enzyme of this pathway, and it catalyzes the cyclization of 3-deoxy-D-arabino-heptulosonate-7-phosphate in 3-dehydroquinate. Here we describe the PCR amplification and cloning of the aroB gene and the overexpression and purification of its product, dehydroquinate synthase, to homogeneity. In order to probe where the recombinant dehydroquinate synthase was active, genetic complementation studies were performed. The Escherichia coli AB2847 mutant was used to demonstrate that the plasmid construction was able to repair the mutants, allowing them to grow in minimal medium devoid of aromatic compound supplementation. In addition, homogeneous recombinant M. tuberculosis dehydroquinate synthase was active in the absence of other enzymes, showing that it is homomeric. These results will support the structural studies with M. tuberculosis dehydroquinate synthase that are essential for the rational design of antimycobacterial agents.