Interaction of the hepatitis B virus protein HBx with the human transcription regulatory protein p120E4F in vitro

dc.creatorRui, E
dc.creatorMoura, PR
dc.creatorGoncalves, KA
dc.creatorRooney, RJ
dc.creatorKobarg, J
dc.date2006
dc.dateJAN
dc.date2014-11-20T03:28:35Z
dc.date2015-11-26T17:13:15Z
dc.date2014-11-20T03:28:35Z
dc.date2015-11-26T17:13:15Z
dc.date.accessioned2018-03-29T00:01:37Z
dc.date.available2018-03-29T00:01:37Z
dc.identifierVirus Research. Elsevier Science Bv, v. 115, n. 1, n. 31, n. 42, 2006.
dc.identifier0168-1702
dc.identifierWOS:000234574400005
dc.identifier10.1016/j.virusres.2005.07.003
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60379
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/60379
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60379
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1281526
dc.descriptionInfection with the hepatitis B virus has been identified as one of the major causes of liver cancer. A large body of experimental work points to a central role for the virally encoded protein HBx in this form of carcinogensis. HBx is expressed in HBV-infected liver cells and interacts with a wide range of cellular proteins, thereby interfering in cellular processes including cell signaling, cycle regulation and apoptosis. In order to identify possible new targets of the HBx protein, we performed a yeast two-hybrid screen using a truncated protein mini-HBx(18-142) as the bait. In addition to known interacting partners, such as RXR and UVDDB 1, we identified several new candidates including the human transcriptional regulatory protein p120E4F, which has been implicated in the regulation of mitosis and the cell cycle. In vitro pull down experiments confirmed the interaction and transcription activation assays in the yeast demonstrated that HBx protein was able to repress GAL4AD-p120E4F-dependent activation of a reporter gene under the control of E4F binding sites found in the adenovirus E4 promoter and the HBV enhancer II region. We also showed that the cysteine residues in HBx are necessary for its interaction with UVDDB1 but not for the interaction with RXR or p120E4F. The possible functional relevance of the interaction between HBx and E4F proteins is discussed in the contexts of cellular transformation and host-virus co-evolution. (c) 2005 Elsevier B.V. All rights reserved.
dc.description115
dc.description1
dc.description31
dc.description42
dc.languageen
dc.publisherElsevier Science Bv
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationVirus Research
dc.relationVirus Res.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjecthepatitis B virus
dc.subjectHBx
dc.subjecthepatocellular carcinoma
dc.subjecttranscription regulation
dc.subjectprotein-protein interaction
dc.subjectOnco-protein
dc.subjectAdenovirus E4 Promoter
dc.subjectDna-binding Activity
dc.subjectRetinoid-x-receptor
dc.subjectTransgenic Mice
dc.subjectTransactivator Protein
dc.subjectEscherichia-coli
dc.subjectHuman Homolog
dc.subjectEnhancer Ii
dc.subjectCell-death
dc.subjectGene
dc.titleInteraction of the hepatitis B virus protein HBx with the human transcription regulatory protein p120E4F in vitro
dc.typeArtículos de revistas


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