单纯疱疹病毒 1 外壳蛋白 pUL36 和 pUL37 的相互作用对于病毒出芽过程中的二次包膜形成是必需的。
The interaction of the HSV-1 tegument proteins pUL36 and pUL37 is essential for secondary envelopment during viral egress.
机构信息
Centre for Virus Research, Westmead Millennium Institute, The University of Sydney and Westmead Hospital, Westmead, NSW 2145, Australia.
Institute of Cell Biology, Hannover Medical School, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany.
出版信息
Virology. 2014 Apr;454-455:67-77. doi: 10.1016/j.virol.2014.02.003. Epub 2014 Feb 22.
The herpes simplex virus type 1 (HSV-1) tegument proteins pUL36 (VP1/2) and pUL37 are essential for viral egress. We previously defined a minimal domain in HSV-1 pUL36, residues 548-572, as important for binding pUL37. Here, we investigated the role of this region in binding to pUL37 and facilitating viral replication. We deleted residues 548-572 in frame in a virus containing a mRFP tag at the N-terminus of the capsid protein VP26 and an eGFP tag at the C-terminus of pUL37 (HSV-1pUL36∆548-572). This mutant virus was unable to generate plaques in Vero cells, indicating that deletion of this region of pUL36 blocks viral replication. Imaging of HSV-1pUL36∆548-572-infected Vero cells, in comparison to parental and resucant, revealed a block in secondary envelopment of cytoplasmic capsids. In addition, immunoblot analysis suggested that failure to bind pUL37 affected the stability of pUL36. This study provides further insight into the role of this essential interaction.
单纯疱疹病毒 1 型 (HSV-1) 的被膜蛋白 pUL36（VP1/2）和 pUL37 对于病毒出芽是必不可少的。我们之前定义了 HSV-1 pUL36 中一个重要的最小结构域，残基 548-572，对与 pUL37 的结合很重要。在这里，我们研究了该区域在与 pUL37 结合和促进病毒复制中的作用。我们在一种病毒中缺失了 548-572 位的框内残基，该病毒在衣壳蛋白 VP26 的 N 端带有 mRFP 标签，在 pUL37 的 C 端带有 eGFP 标签（HSV-1pUL36∆548-572）。该突变病毒无法在 Vero 细胞中产生蚀斑，表明 pUL36 该区域的缺失阻断了病毒复制。与亲本和拯救病毒相比，对 HSV-1pUL36∆548-572 感染的 Vero 细胞进行成像，发现细胞质衣壳的二次包膜被阻断。此外，免疫印迹分析表明，不能与 pUL37 结合会影响 pUL36 的稳定性。这项研究进一步深入了解了这一重要相互作用的作用。
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