The pattern of tegument-capsid interaction in the herpes simplex virus type 1 virion is not influenced by the small hexon-associated protein VP26
The pattern of tegument-capsid interaction in the herpes simplex virus type 1 virion is not influenced by the small hexon-associated protein VP26
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DOI：
10.1128/jvi.75.23.11863-11867.2001
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发表时间：
2001-12-01
影响因子：
5.4
通讯作者：
Rixon, FJ
中科院分区：
文献类型：
--
作者：
Chen, DH;Jakana, J;Rixon, FJ
对完整的1型单纯疱疹病毒（HSV-1）病毒粒子的三维结构检查显示，被膜和衣壳之间的二十面体对称相互作用涉及五边形而不包括六边形（Z. H. Zhou， D. H. Chen， J. Jakana， F. J. Rixon， W. Chin， J. Virol. 73:3210-3218, 1999）。为了解释这一点，我们假设小衣壳蛋白VP26的存在掩盖了潜在的结合位点并阻止了被皮附着。我们现在通过确定缺乏VP26的病毒粒子的结构来验证这一假设。除了衣壳明显缺乏VP26外，VP26负型病毒粒子和野生型病毒粒子的结构基本相同。值得注意的是，它们显示出相同的被毛附着模式，从而表明VP26不是五边形和六边形的不同被毛结合特性的原因。
Examination of the three-dimensional structure of intact herpes simplex virus type 1 (HSV-1) virions had revealed that the icosahedrally symmetrical interaction between the tegument and capsid involves the pentons but not the hexons (Z. H. Zhou, D. H. Chen, J. Jakana, F. J. Rixon, and W. Chin, J. Virol. 73:3210-3218, 1999). To account for this, we postulated that the presence of the small capsid protein, VP26, on top of the hexons was masking potential binding sites and preventing tegument attachment. We have now tested this hypothesis by determining the structure of virions lacking VP26. Apart from the obvious absence of VP26 from the capsids, the structures of the VP26 minus and wild-type virions were essentially identical. Notably, they showed the same tegument attachment patterns, thereby demonstrating that VP26 is not responsible for the divergent tegument binding properties of pentons and hexons.