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Recombinant Cry3Aa has insecticidal activity against the andean potato weevil, Premnotrypes Vorax

dc.contributor.authorHernández-Fernández, Javier Adolfo
dc.creatorGómez, Sylvia
dc.creatorMateus, Ana Constanza
dc.creatorZimmermann, Barbara H.
dc.date.accessioned2024-04-03T10:02:20Z
dc.date.available2024-04-03T10:02:20Z
dc.date.created2000-11
dc.description.abstractEl gorgojo andino de la papa, Premnotrypes vorax, un insecto del orden Coleoptera, es una de las principales causas de daño a los cultivos de papa en las regiones andinas de América del Sur. Las proteínas Cry insecticidas de Bacillus thuringiensis son pesticidas biológicos útiles, y algunas son tóxicas para los insectos coleópteros. Se sobreexpresó la proteína Cry3Aa recombinante etiquetada con histidina en células hospedadoras de Escherichia coli. La proteína recombinante se solubilizó a un pH alto con urea, se purificó utilizando resina de afinidad de nitrilotriacetato de Ni^21^ y se dializó para bajar el pH y eliminar la urea. Se realizaron bioensayos con un medio para insectos cuya superficie estaba impregnada con 70 mg/mL de toxinas nativas o recombinantes purificadas. Las larvas de primer estadio expuestas al medio tratado con toxina durante 5 días exhibieron mortalidades del 57% (Cry3Aa nativa) al 52% (Cry3Aa recombinante). Las proteínas Cry3Aa nativas y recombinantes purificadas parecieron ser igualmente tóxicas para el gorgojo andino de la papa.spa
dc.description.abstractenglishThe Andean potato weevil, Premnotrypes vorax, an insect of the order Coleoptera, is a major cause of damage to potato crops in the Andean regions of South America. The insecticidal Cry proteins from Bacillus thuringiensis are useful biological pesticides, and some are toxic to Coleopteran insects. We overexpressed recombinant, histidine-tagged Cry3Aa protein in Escherichia coli host cells. The recombinant protein was solubilized at high pH with urea, purified using Ni21-nitrilo-triacetic acid affinity resin, and dialysed to lower pH and remove urea. Bioassays were performed with an insect media whose surface was spread with 70 mg/mL purified native or recombinant toxins. First instar larvae exposed to toxin treated media for 5 days exhibited mortalities from 57% (native Cry3Aa) to 52% (recombinant Cry3Aa). Purified native and recombinant Cry3Aa proteins appeared to be equally toxic to the Andean potato weevil.spa
dc.description.hashtag#Cry3Aaspa
dc.description.hashtag#Recombinantespa
dc.description.hashtag#Insecticidaspa
dc.description.hashtag#Gorgojoandinospa
dc.description.hashtag#Papaspa
dc.description.hashtag#Premnotrypesvoraxspa
dc.format.extent653–656 páginasspa
dc.format.mimetypeapplication/pdfspa
dc.identifier.otherhttps://www.researchgate.net/publication/12210874_Recombinant_Cry3Aa_Has_Insecticidal_Activity_against_the_Andean_Potato_Weevil_Premnotrypes_voraxspa
dc.identifier.urihttps://hdl.handle.net/20.500.12010/34173
dc.language.isospaspa
dc.publisherBiochemical and Biophysical Research Communications Volumen 279spa
dc.relation.references1. Alcazar, J., and Cisneros, F. (posted 1996) Integrated Management for Andean potato weevils in pilot units. The International Potato Center (CIP). Available at http://www.cipotato.org/new/ WebProRep96/program4/prog43.htm.spa
dc.relation.references2. Bravo, A. (1997) Phylogenetic relationships of Bacillus thuringiensis delta-endotoxin family proteins and their functional domains. J. Bacteriol. 179, 2793–2801spa
dc.relation.references3. Hofte, H., and Whiteley, H. R. (1989) Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol. Rev. 53, 242–255.spa
dc.relation.references4. Schnepf, E., Crickmore, N., Van Rie, J., Lereclus, D., Baum, J., Feitelson, J., Zeigler, D. R., and Dean, D. H. (1998) Bacillus thuringiensis and its pesticidal crystal proteins. Microbiol. Mol. Biol. Rev. 62, 775–806.spa
dc.relation.references5. Crickmore, N. 21 (posted July 1999) Bt Toxin Nomenclature. Available at http://www.biols.susx.ac.uk/Home/Neil_Crickmore/ Bt/index.hml.spa
dc.relation.references7. Hofte, H., Seurinck, J., Van Houtven, A., and Vaeck, M. (1987) Nucleotide sequence of a gene encoding an insecticidal protein of Bacillus thuringiensis var. tenebrionis toxic against Coleoptera. Nucleic. Acids. Res. 15, 7183.spa
dc.relation.references8. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254.spa
dc.relation.references9. Koller, C. N., Bauer, L. S., and Hollingworth, R. M. (1992) Characterization of the pH-mediated solubility of Bacillus thuringiensis var. san diego native delta endotoxin crystal. Biochim. Biophys. Res. Comm. 184, 692–699.spa
dc.relation.references10. Grayson, D. R., Lee, L., and Evans, D. R. (1985) Immunochemical analysis of the domain structure of CAD, the multifunctional protein that initiates pyrimidine biosynthesis in mammalian cells. J. Biol. Chem. 260, 15840–15849.spa
dc.relation.references11. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.spa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.localAbierto (Texto Completo)spa
dc.subjectCry3Aaspa
dc.subjectCry3Aspa
dc.subjectPremnotrypes voraxspa
dc.subjectGorgojo andino de la papaspa
dc.subjectBacillus thuringiensisspa
dc.subject.keywordCry3Aaspa
dc.subject.keywordCry3Aspa
dc.subject.keywordPremnotrypes voraxspa
dc.subject.keywordAndean potato weevilspa
dc.subject.keywordBacillus thuringiensisspa
dc.subject.lembGorgojo andino de la papa -- Premnotrypes vorax -- Control biológicospa
dc.subject.lembProteínas Cry -- Pesticidas biológicosspa
dc.subject.lembManejo integrado de plagas -- Métodos de contolspa
dc.subject.lembCultivo de papa -- Biotecnología agrícolaspa
dc.titleRecombinant Cry3Aa has insecticidal activity against the andean potato weevil, Premnotrypes Voraxspa
dc.type.coarhttp://purl.org/coar/resource_type/c_6501spa
dspace.entity.typePublication
relation.isAuthorOfPublication22c0e1d7-3e57-4ff1-8db2-7f60bee18bfc
relation.isAuthorOfPublication.latestForDiscovery22c0e1d7-3e57-4ff1-8db2-7f60bee18bfc

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