State Key Laboratory of Biocontrol, Sun Yat-sen University, Guangzhou 510275, China.
Virus Res. 2010 May;149(2):241-4. doi: 10.1016/j.virusres.2010.01.020. Epub 2010 Feb 6.
Core protein of hepatitis B virus (HBV) with various C-terminal lengths (residue 154, 164, 167 and 183) can self-assemble into recombinant hepatitis B core antigen (HBcAg) particles. To understand the RNA encapsidation mechanism of HBV, the three-dimensional structures of these particles were reconstructed by cryo-electron microscopy (cryoEM). Detailed structural comparisons showed that their capsid structures are highly similar, while the RNA content is increased upon the retention of more amino acid residues at the C-terminus of core protein, suggesting the crucial role of the basic C-terminal tail on determining the genome size.
乙肝病毒（HBV）的核心蛋白带有不同的 C 末端长度（残基 154、164、167 和 183），可以自行组装成重组乙型肝炎核心抗原（HBcAg）颗粒。为了了解 HBV 的 RNA 包裹机制，通过冷冻电镜（cryoEM）重建了这些颗粒的三维结构。详细的结构比较表明，它们的衣壳结构高度相似，而当核心蛋白的 C 末端保留更多的氨基酸残基时，RNA 含量会增加，这表明碱性 C 末端尾巴在决定基因组大小时起着关键作用。
