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Journal of Virology, November 1998, p. 9359-9364, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Metabolic Labeling of Woodchuck Hepatitis B Virus X Protein in Naturally Infected Hepatocytes Reveals a Bimodal Half-Life and Association with the Nuclear Framework

Maura Dandri,1,2 Joerg Petersen,1,2,3 Richard J. Stockert,1 Thomas M. Harris,1 and Charles E. Rogler1,*

Marion Bessin Liver Research Center, Department of Medicine, Jack and Pearl Resnick Campus of the Albert Einstein College of Medicine, Bronx, New York 10461,1 and Heinrich-Pette Institut for Experimental Virology and Immunology at the University of Hamburg2 and Department of Medicine, University of Hamburg,3 Hamburg, Germany

Received 10 April 1998/Accepted 22 July 1998

In order to identify potential sites of hepadnavirus X protein action, we have investigated the subcellular distribution and the stability of woodchuck hepatitis virus (WHV) X protein (WHx) in primary hepatocytes isolated from woodchucks with persistent WHV infection. In vivo cell labeling and cell fractionation studies showed that the majority of WHx is a soluble cytoplasmic protein while a minor part of newly synthesized WHx is associated with a nuclear framework fraction (20%) and with cytoskeletal components (5 to 10%). Pulse-chase experiments revealed that cytoplasmic WHx has a short half-life and decays with bimodal kinetics (approximately 20 min and 3 h). The rates of association and turnover of nucleus-associated WHx suggest that compartmentalization may be responsible for the bimodal turnover observed in the cytoplasm.

* Corresponding author. Mailing address: M. Bessin Liver Research Center, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Phone: (718) 430-2607. Fax: (718) 430-8975. E-mail: crogler{at}aecom.yu.edu.

Journal of Virology, November 1998, p. 9359-9364, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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