Seifer M, Standring D N
Hormone Research Institute, University of California at San Francisco, USA.
Intervirology. 1995;38(1-2):47-62. doi: 10.1159/000150414.
Recent studies in Xenopus oocytes and other systems have led to an understanding of the HBV capsid, or core particle, assembly process. Nascent HBV core polypeptides rapidly dimerize. Accumulation of free dimers to a signature concentration (approximately 0.8 microM) then triggers a highly cooperative capsid assembly reaction. This dimer-to-capsid transition is accompanied by a switch from HBe to HBc antigenicity and appears to be nucleated by interaction between core protein and RNA: deletion of a protamine-like RNA binding domain at the C-terminus of the core protein markedly increases the concentration of dimers needed to drive capsid assembly. The simple assembly pathway seen for HBV capsids mirrors that of R17 bacteriophage.
近期对非洲爪蟾卵母细胞及其他系统的研究使人们对乙肝病毒衣壳（即核心颗粒）的组装过程有了一定认识。新生的乙肝病毒核心多肽会迅速二聚化。游离二聚体积累至特定浓度（约0.8微摩尔）时，会引发高度协同的衣壳组装反应。这种从二聚体到衣壳的转变伴随着从HBe抗原性到HBc抗原性的转换，且似乎由核心蛋白与RNA之间的相互作用引发成核：核心蛋白C端类似鱼精蛋白的RNA结合结构域缺失会显著提高驱动衣壳组装所需的二聚体浓度。乙肝病毒衣壳呈现的简单组装途径与R17噬菌体的相似。
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