Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: Expression and spectroscopic analysis of a mutant hepatitis B virus onco-protein HBx without cysteine residues
Author: Rui, E
de Moura, PR
Goncalves, KD
Kobarg, J
Abstract: Chronic 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.
Subject: viral hepatitis
hepatitis B virus X protein
viral transactivator
circular dichroism
Country: Holanda
Editor: Elsevier Science Bv
Citation: Journal Of Virological Methods. Elsevier Science Bv, v. 126, n. 41671, n. 65, n. 74, 2005.
Rights: fechado
Identifier DOI: 10.1016/j.jviromet.2005.01.022
Date Issue: 2005
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000229003000008.pdf375.27 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.