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Journal of Virology, December 2007, p. 13218-13229, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.00846-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

A Structural Model for Duck Hepatitis B Virus Core Protein Derived by Extensive Mutagenesis ^,

University Hospital Freiburg, Internal Medicine 2/Molecular Biology, Hugstetter Str. 55, D-79106 Freiburg, Germany,¹ European Molecular Biology Laboratory, Meyerhofstr. 1, D-69117 Heidelberg, Germany²

Received 20 April 2007/ Accepted 11 September 2007

Duck hepatitis B virus (DHBV) shares many fundamental features with human HBV. However, the DHBV core protein (DHBc), forming the nucleocapsid shell, is much larger than that of HBV (HBc) and, in contrast to HBc, there is little direct information on its structure. Here we applied an efficient expression system for recombinant DHBc particles to the biochemical analysis of a large panel of mutant DHBc proteins. By combining these data with primary sequence alignments, secondary structure prediction, and three-dimensional modeling, we propose a model for the fold of DHBc. Its major features are a HBc-like two-domain structure with an assembly domain comprising the first about 185 amino acids and a C-terminal nucleic acid binding domain (CTD), connected by a morphogenic linker region that is longer than in HBc and extends into the CTD. The assembly domain shares with HBc a framework of four major -helices but is decorated at its tip with an extra element that contains at least one helix and that is made up only in part by the previously predicted insertion sequence. All subelements are interconnected, such that structural changes at one site are transmitted to others, resulting in an unexpected variability of particle morphologies. Key features of the model are independently supported by the accompanying epitope mapping study. These data should be valuable for functional studies on the impact of core protein structure on virus replication, and some of the mutant proteins may be particularly suitable for higher-resolution structural investigations.

Published ahead of print on 19 September 2007.

Supplemental material for this article may be found at http://jvi.asm.org/.

This article has been cited by other articles:

• Vorreiter, J., Leifer, I., Rosler, C., Jackevica, L., Pumpens, P., Nassal, M. (2007). Monoclonal Antibodies Providing Topological Information on the Duck Hepatitis B Virus Core Protein and Avihepadnaviral Nucleocapsid Structure. J. Virol. 81: 13230-13234 [Abstract] [Full Text]