Expression and spectroscopic analysis of a mutant hepatitis B virus onco-protein HBx without cysteine residues

dc.creatorRui, E
dc.creatorde Moura, PR
dc.creatorGoncalves, KD
dc.creatorKobarg, J
dc.date2005
dc.dateJUN
dc.date2014-11-18T03:05:16Z
dc.date2015-11-26T17:45:38Z
dc.date2014-11-18T03:05:16Z
dc.date2015-11-26T17:45:38Z
dc.date.accessioned2018-03-29T00:28:00Z
dc.date.available2018-03-29T00:28:00Z
dc.identifierJournal Of Virological Methods. Elsevier Science Bv, v. 126, n. 41671, n. 65, n. 74, 2005.
dc.identifier0166-0934
dc.identifierWOS:000229003000008
dc.identifier10.1016/j.jviromet.2005.01.022
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/66456
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/66456
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/66456
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1288239
dc.descriptionChronic infection of the hepatitis B virus (HBV) is one of the causes leading to liver cancer. The 3.2 kb genome of HBV encodes four proteins: core antigen, surface antigen, a DNA polymerase and the X protein (HBx). The biological functions of HBx are not fully understood. It has been shown that HBx is a potent trans -activator, which activates transcription of many cellular and viral promoters indirectly via protein-protein interactions. These transactivating activities of HBx may contribute to the development of hepatocellular carcinoma. In this paper a truncated mini-HBx(-Cys) ( 18-142) protein, where the cysteines had been either deleted or substituted by serines, was constructed by site-directed mutagenesis and overexpressed as a 6xHis fusion protein in Escherichia coli. The 6xHis-mini-HBx(-Cys) protein was isolated from inclusion bodies, purified by Ni-affinity chromatography under denaturing conditions and refolded by sequential dialysis. The structure of the 6xHis-mini-HBx(-Cys) protein was analyzed by circular dichroism, fluorescence and one-dimensional NMR spectroscopic assays. The data presented here suggest that HBx is unstructured but has a propensity to gain secondary structure under specific experimental conditions. Its conformational flexibility might partially explain its functional complexity, namely its capacity to interact with a wide array of signaling proteins, transcriptional regulators and nucleic acids. © 2005 Elsevier B.V. All rights reserved.
dc.description126
dc.description41671
dc.description65
dc.description74
dc.languageen
dc.publisherElsevier Science Bv
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationJournal Of Virological Methods
dc.relationJ. Virol. Methods
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectviral hepatitis
dc.subjecthepatitis B virus X protein
dc.subjectviral transactivator
dc.subjectonco-protein
dc.subjectcircular dichroism
dc.subjectfluorescence
dc.subjectTata-binding Protein
dc.subjectLong Terminal Repeat
dc.subjectRetinoid-x-receptor
dc.subjectHepatocellular-carcinoma
dc.subjectDna-binding
dc.subjectEscherichia-coli
dc.subjectTransactivator Protein
dc.subjectViral-infection
dc.subjectDamaged Dna
dc.subjectLiver-cells
dc.titleExpression and spectroscopic analysis of a mutant hepatitis B virus onco-protein HBx without cysteine residues
dc.typeArtículos de revistas


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