Cloning, expression, and purification of the virulence-associated protein D from Xylella fastidiosa

dc.creatorCatani, CF
dc.creatorAzzoni, AR
dc.creatorPaula, DP
dc.creatorTada, SFS
dc.creatorRosselli, LK
dc.creatorde Souza, AP
dc.creatorYano, T
dc.date2004
dc.dateOCT
dc.date2014-11-16T23:14:31Z
dc.date2015-11-26T16:31:46Z
dc.date2014-11-16T23:14:31Z
dc.date2015-11-26T16:31:46Z
dc.date.accessioned2018-03-28T23:12:57Z
dc.date.available2018-03-28T23:12:57Z
dc.identifierProtein Expression And Purification. Academic Press Inc Elsevier Science, v. 37, n. 2, n. 320, n. 326, 2004.
dc.identifier1046-5928
dc.identifierWOS:000224166400008
dc.identifier10.1016/j.pep.2004.07.002
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/56108
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/56108
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/56108
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1270308
dc.descriptionin this study, an efficient expression system, based on the pET32Xa/LIC vector, for producing a Xylella fastidiosa virulence-associated protein D, found to have a strong similarity to Riemerella anatipestifer and Actinobacillus actinomycetencomitans VapD protein, is presented. The protein has a molecular mass of 17.637 Da and a calculated pI of 5.49. The selected XFa0052 gene was cloned in the pET32Xa/LIC vector and the plasmid was transformed into Escherichia coli BL21 (DE3) strain at 37degreesC. with an induction time of 2 h and 1 mM IPTG concentration. The protein present in the soluble fraction was purified by immobilized metal affinity chromatography (IMAC), and had its identity determined by mass spectrometry (MALDI-TOF) and N-terminal sequencing. The purified protein was found as a single band on SDS-PAGE and its correct folding was verified by circular dichroism spectroscopy. (C) 2004 Elsevier Inc. All rights reserved.
dc.description37
dc.description2
dc.description320
dc.description326
dc.languageen
dc.publisherAcademic Press Inc Elsevier Science
dc.publisherSan Diego
dc.publisherEUA
dc.relationProtein Expression And Purification
dc.relationProtein Expr. Purif.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectVapD protein
dc.subjectexpression and purification
dc.subjectXylella fastidiosa
dc.subjectRhodococcus-equi
dc.subjectGenetic Organization
dc.subjectDichelobacter-nodosus
dc.subjectPierces-disease
dc.subjectPlasmid
dc.subjectGenome
dc.subjectPathogenicity
dc.subjectSequence
dc.subjectRegion
dc.subjectSurvival
dc.titleCloning, expression, and purification of the virulence-associated protein D from Xylella fastidiosa
dc.typeArtículos de revistas


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