This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Seifer, M Articles by Standring, D N Search for Related Content PubMed PubMed Citation Articles by Seifer, M Articles by Standring, D N

A micromolar pool of antigenically distinct precursors is required to initiate cooperative assembly of hepatitis B virus capsids in Xenopus oocytes.

Hormone Research Institute, University of California, San Francisco 94143-0534.

ABSTRACT

Assembly of hepatitis B virus capsid-like (core) particles occurs efficiently in a variety of heterologous systems via aggregation of approximately 180 molecules of a single 21.5-kDa core protein (p21.5), resulting in an icosahedral capsid structure with T = 3 symmetry. Recent studies on the assembly of hepatitis B virus core particles in Xenopus oocytes suggested that dimers of p21.5 represent the major building block from which capsids are generated. Here we determined the concentration dependence of this assembly process. By injecting serially diluted synthetic p21.5 mRNA into Xenopus oocytes, we expressed different levels of intracellular p21.5 and monitored the production of p21.5 dimers and capsids by radiolabeling and immunoprecipitation, by radioimmunoassay, or by quantitative enzyme-linked immunosorbent assay analysis. The data revealed that (i) p21.5 dimers and capsids are antigenically distinct, (ii) capsid assembly is a highly cooperative and concentration-dependent process, and (iii) p21.5 must accumulate to a signature concentration of approximately 0.7 to 0.8 microM before capsid assembly initiates. This assembly process is strikingly similar to the assembly of RNA bacteriophage R17 as defined by in vitro studies.

This article has been cited by other articles:

• Keasler, V. V., Hodgson, A. J., Madden, C. R., Slagle, B. L. (2007). Enhancement of Hepatitis B Virus Replication by the Regulatory X Protein In Vitro and In Vivo. J. Virol. 81: 2656-2662 [Abstract] [Full Text]  
• Rabe, B., Vlachou, A., Pante, N., Helenius, A., Kann, M. (2003). Nuclear import of hepatitis B virus capsids and release of the viral genome. Proc. Natl. Acad. Sci. USA 100: 9849-9854 [Abstract] [Full Text]  
• Yao, E., Tavis, J. E. (2003). Kinetics of Synthesis and Turnover of the Duck Hepatitis B Virus Reverse Transcriptase. J. Biol. Chem. 278: 1201-1205 [Abstract] [Full Text]  
• Endres, D., Zlotnick, A. (2002). Model-Based Analysis of Assembly Kinetics for Virus Capsids or Other Spherical Polymers. Biophys. J 83: 1217-1230 [Abstract] [Full Text]  
• Zlotnick, A., Ceres, P., Singh, S., Johnson, J. M. (2002). A Small Molecule Inhibits and Misdirects Assembly of Hepatitis B Virus Capsids. J. Virol. 76: 4848-4854 [Abstract] [Full Text]  
• Yao, E., Gong, Y., Chen, N., Tavis, J. E. (2000). The Majority of Duck Hepatitis B Virus Reverse Transcriptase in Cells Is Nonencapsidated and Is Bound to a Cytoplasmic Structure. J. Virol. 74: 8648-8657 [Abstract] [Full Text]  
• Guidotti, L. G., Eggers, C. M., Raney, A. K., Chi, S. Y., Peters, J. M., Gonzalez, F. J., McLachlan, A. (1999). In Vivo Regulation of Hepatitis B Virus Replication by Peroxisome Proliferators. J. Virol. 73: 10377-10386 [Abstract] [Full Text]  
• Kann, M., Sodeik, B., Vlachou, A., Gerlich, W. H., Helenius, A. (1999). Phosphorylation-dependent Binding of Hepatitis B Virus Core Particles to the Nuclear Pore Complex. J. Cell Biol. 145: 45-55 [Abstract] [Full Text]  
• Koschel, M., Thomssen, R., Bruss, V. (1999). Extensive Mutagenesis of the Hepatitis B Virus Core Gene and Mapping of Mutations That Allow Capsid Formation. J. Virol. 73: 2153-2160 [Abstract] [Full Text]  
• Conway, J. F., Cheng, N., Zlotnick, A., Stahl, S. J., Wingfield, P. T., Steven, A. C. (1998). Localization of the N terminus of hepatitis B virus capsid protein by peptide-based difference mapping from cryoelectron microscopy. Proc. Natl. Acad. Sci. USA 95: 14622-14627 [Abstract] [Full Text]  
• Konig, S., Beterams, G., Nassal, M. (1998). Mapping of Homologous Interaction Sites in the Hepatitis B Virus Core Protein. J. Virol. 72: 4997-5005 [Abstract] [Full Text]