Effect of Staurosporine on the Intracellular Localization of Hepatitis B Virus Core Protein

• Main Authors: Aris Haryanto, Nastiti Wijayanti, Michael Kann
• Format: Article
• Language: English
• Published: Universitas Gadjah Mada, Yogyakarta 2015-11-01
• Series: Indonesian Journal of Biotechnology
• Online Access: http://journal.ugm.ac.id/ijbiotech/article/view/7767

protein is also including in the HBV genome targeting into the nucleus through modulating carboxyl residues by<br />phosphorylation. Nuclear localication Signal (NLS) in HBV core protein is inside the virion structure and it must be<br />unmasked in order to function, perhaps by phosphorylation. Phosphorylation of of HBV core protein in turn could<br />begin to alter capsid conformation. Staurosporine is a natural product originally isolated from bacterium<br />Streptomyces staurosporeus. Staurosporine was discovered to have biological activities ranging from anti-fungal to<br />anti-hypertensive. The interest in these activities resulted in a large investigative effort in chemistry and biology and<br />the discovery of the potential for anti-cancer treatment. The main biological activity of Staurosporine is the inhibition<br />of protein kinases through the prevention of ATP binding to the kinase. In the present study, we have studied the<br />intracellular localization of EGFP-Core fusion protein with triple HBV core and SV-40 nuclear localization signal at<br />its carboxyl terminal in presence and absence of Staurosporine. We also to study the effect of Staurosporine treatment<br />on the intracellular localization of EGFP-Core fusion protein in the hepatocyte cells line of HepG2 cell. Results<br />showed that effect of Staurosporine is prevent the nuclear localization of EGFP-Core fusion protein into nucleus<br />through an inhibition of the phosphorylation of core protein. Stauroporine also prevents cell division so that passive<br />trapping of core protein is inhibited.