The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins
The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins
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DOI：
10.1128/jvi.01113-07
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发表时间：
2007-11-01
影响因子：
5.4
通讯作者：
Smith, Gregory Allan
中科院分区：
文献类型：
--
作者：
Coller, Kelly Elizabeth;Lee, Joy I-Hsuan;Smith, Gregory Allan
疱疹病毒衣壳如何获得被膜蛋白仍然是病毒组装中的关键问题。使用伪狂犬病病毒（PRV），我们以前已经表明，62个羧基末端氨基酸的VP 1/2大被膜蛋白是必不可少的病毒繁殖和瞬时表达时，融合到绿色荧光蛋白重新定位到核衣壳装配病毒感染后。在这里，我们表明，本地化的VP 1/2衣壳结合结构域（VP 1/2cbd）到peptilions是保守的单纯疱疹病毒I型（HSV-1），这种招聘是专门对衣壳。使用突变病毒筛选，我们发现UL 25基因的蛋白产物是VP 1/2cbd与衣壳结合所必需的。UL 25与VP 1/2之间存在相互作用。通过来自瞬时表达HSV-1或PRV蛋白的细胞的免疫共沉淀证实。综上所述，这些发现表明，VP 1/2羧基末端的基本功能是将VP 1/2被膜蛋白锚在衣壳上。此外，UL 25编码一种多功能衣壳蛋白，其不仅参与如前所述的衣壳化，而且还参与盖层化。
How alphaherpesvirus capsids acquire tegument proteins remains a key question in viral assembly. Using pseudorabies virus (PRV), we have previously shown that the 62 carboxy-terminal amino acids of the VP1/2 large tegument protein are essential for viral propagation and when transiently expressed as a fusion to green fluorescent protein relocalize to nuclear capsid assemblons following viral infection. Here, we show that localization of the VP1/2 capsid-binding domain (VP1/2cbd) into assemblions is conserved in herpes simplex virus type I (HSV-1) and that this recruitment is specifically on capsids. Using a mutant virus screen, we find that the protein product of the UL25 gene is essential for VP1/2cbd association with capsids. An interaction between UL25 and VP1/2 was. corroborated by coimmunoprecipitation from cells transiently expressing either HSV-1 or PRV proteins. Taken together, these findings suggest that the essential function of the VP1/2 carboxy terminus is to anchor the VP1/2 tegument protein to capsids. Furthermore, UL25 encodes a multifunctional capsid protein involved in not only encapsidation, as previously described, but also tegumentation.