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Journal of Virology, December 2007, p. 13230-13234, Vol. 81, No. 23
0022-538X/07/$08.00+0 doi:10.1128/JVI.00847-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
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University Hospital Freiburg, Internal Medicine 2/Molecular Biology, Hugstetter Str. 55, D-79106 Freiburg, Germany,1 Latvian Biomedical Research and Study Centre, Ratsupites Str. 1, Riga, LV-1067, Latvia2
Received 20 April 2007/ Accepted 11 September 2007
The icosahedral capsid of duck hepatitis B virus (DHBV) is formed by a single core protein species (DHBc). DHBc is much larger than HBc from human HBV, and no high-resolution structure is available. In an accompanying study (M. Nassal, I. Leifer, I. Wingert, K. Dallmeier, S. Prinz, and J. Vorreiter, J. Virol. 81:13218-13229, 2007), we used extensive mutagenesis to derive a structural model for DHBc. For independent validation, we here mapped the epitopes of seven anti-DHBc monoclonal antibodies. Using numerous recombinant DHBc proteins and authentic nucleocapsids from different avihepadnaviruses as test antigens, plus a panel of complementary assays, particle-specific and exposed plus buried linear epitopes were revealed. These data fully support key features of the model.
Published ahead of print on 19 September 2007.
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