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Expression, purification and crystallization of the hepatitis b virus protein HBX for its structural analysis by X-ray diffraction


The short genome of the Hepatitis B virus (HBV) encodes for only four proteins. One of them, the protein HBx, is implicated in the regulation of the viral life cycle and is required for the infectivity of the virus in vivo. Although pleiotropic effects of this protein have been described in vitro, the definite function of this protein remains to be determined. It is however clear that HBx is involved in the progression from chronic hepatitis to hepatocellular carcinoma (HCC). In the present investigation it is intended to address the unknown three-dimensional structure of the HBx protein. To this end the HBx will be expressed in bacterial as well as eucaryotic hosts and purified in large quantities so that the protein can be crystallized for the determination of its structure by X-ray diffraction analysis at the LNLS in Campinas. The knowledge of the HBx structure will be of great help not only for the better characterization of its function in the progression of the HBV dependent liver carcinoma but will also allow the rational design of small molecular compounds that can inhibit this process The development of such drugs would be of great use to improve the health status of the over 10% of the world wide population that is infected with the HBV virus. (AU)

Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
RUI, EDMILSON; MOURA, PATRICIA RIBEIRO DE; GONÇALVES, KALIANDRA DE ALMEIDA; KOBARG, JÖRG. Expression and spectroscopic analysis of a mutant hepatitis B virus onco-protein HBx without cysteine residues. Journal of Virological Methods, v. 126, n. 1/2, p. 65-74, June 2005.
DE MOURA‚ P.R.; RUI‚ E.; DE ALMEIDA GONÇALVES‚ K.; KOBARG‚ J. The cysteine residues of the hepatitis B virus onco-protein HBx are not required for its interaction with RNA or with human p53. VIRUS RESEARCH, v. 108, n. 1, p. 121-131, 2005.

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