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Expression of disease resistance in genetically modified grapevines correlates with the contents of viral sequences in the T-DNA and global genome methylation. Repositório Alice
BOSCO, D. D.; SINSKI, I.; RITSCHEL, P. S.; CAMARGO, U. A.; FAJARDO, T. V. M.; HARAKAVA, R.; QUECINI, V..
Abstract Increased tolerance to pathogens is an important goal in conventional and biotechnology-assisted grapevine breeding programs worldwide. Fungal and viral pathogens cause direct losses in berry production, but also affect the quality of the final products. Precision breeding strategies allow the introduction of resistance characters in elite cultivars, although the factors determining the plant?s overall performance are not fully characterized. Grapevine plants expressing defense proteins, from fungal or plant origins, or of the coat protein gene of grapevine leafroll-associated virus 3 (GLRaV-3) were generated by Agrobacterium -mediated transformation of somatic embryos and shoot apical meristems. The responses of the transformed lines to pathogen...
Tipo: Artigo em periódico indexado (ALICE) Palavras-chave: Pathogenesis related protein 5; Fungus; Chitinase; Epigenetics; Grapevine leafroll-associated virus 3; Vitis.
Ano: 2018 URL: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1092380
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Expression of grapevine leafroll-associated virus 3 coat protein gene in Escherichia coli and production of polyclonal antibodies. Repositório Alice
FAJARDO, T. V. M.; BARROS, D. R.; NICKEL, O.; KUHN, G.; ZERBINI, M..
Grapevine leafroll-associated virus 3 (GLRaV-3), the main viral species ofthe grapevine leafroll complex, causes yield and quality reduction in grapes (Vitis spp.). The coat protein gene was RT-PCR-amplified from total RNA extracted from infected grapevine leaves and the amplified fragment was cloned and completely sequenced. The fragment was subsequently subcloned into the pRSET-C expression vector. The recombinant plasmid was used to transform Escherichia coli BL21 :DE3 and express the capsid protein. The coat protein, fused to a 6 His-tag, was purified by affinity chromatography using an Ni-NTA resin. The identity ofthe purified protein was confirmed by SDS-PAGE and Westem blot. The in vitro-expressed protein was quantified and used for rabbit...
Tipo: Artigo em periódico indexado (ALICE) Palavras-chave: Enrolamento da folha da videira; Proteína recombinante; Sorologia; Anticorpo; Doença de Planta; Uva; Vírus; Viticultura; Grapevine leafroll-associated virus 3.
Ano: 2007 URL: http://www.alice.cnptia.embrapa.br/alice/handle/doc/542752
Registros recuperados: 2
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