Vorreiter Jolanta, Leifer Immanuel, Rösler Christine, Jackevica Ludmila, Pumpens Paul, Nassal Michael
University Hospital Freiburg, Internal Medicine 2/Molecular Biology, Hugstetter Str. 55, D-79106 Freiburg, Germany.
J Virol. 2007 Dec;81(23):13230-4. doi: 10.1128/JVI.00847-07. Epub 2007 Sep 19.
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.
鸭乙型肝炎病毒(DHBV)的二十面体衣壳由单一核心蛋白种类(DHBc)构成。DHBc比人乙肝病毒的乙肝核心蛋白(HBc)大得多,且尚无高分辨率结构。在一项配套研究(M. Nassal、I. Leifer、I. Wingert、K. Dallmeier、S. Prinz和J. Vorreiter,《病毒学杂志》81:13218 - 13229,2007年)中,我们通过广泛诱变得出了DHBc的结构模型。为进行独立验证,我们在此绘制了七种抗DHBc单克隆抗体的表位图谱。使用来自不同禽嗜肝DNA病毒的大量重组DHBc蛋白和真实核衣壳作为测试抗原,再加上一组互补检测方法,揭示了颗粒特异性以及暴露和埋藏的线性表位。这些数据充分支持了该模型的关键特征。