The conserved carboxyl terminus of human parainfluenza virus type 2 V protein plays an important role in virus growth.
The conserved carboxyl terminus of human parainfluenza virus type 2 V protein plays an important role in virus growth.
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DOI：
10.1016/j.virol.2006.12.017
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发表时间：
2007-05
期刊：
影响因子：
3.7
通讯作者：
M. Nishio;M. Tsurudome;H. Ishihara;Morihiro Ito;Yasuhiko Ito
中科院分区：
文献类型：
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作者：
M. Nishio;M. Tsurudome;H. Ishihara;Morihiro Ito;Yasuhiko Ito
我们之前的研究结果表明，人副流感病毒2型（hPIV2） V蛋白特异性结构域的一些残基不仅对STAT蛋白降解至关重要，而且对促进病毒生长也至关重要。在这里，我们证明了这些表达突变V蛋白的重组hpiv2 （rPIV2）的病毒生长在短暂表达野生型V蛋白的HeLa细胞中得到改善，而在组成型表达V蛋白的细胞中则没有改善。因此，我们确定了V蛋白的区域，该区域对其寡聚化和与NP蛋白形成复合物至关重要。我们还发现了一个宿主蛋白AlP1/Alix，作为V和NP蛋白的相互作用伙伴，参与了几种包膜病毒的凋亡和有效出芽。用小干扰RNA去除AIP1/Alix抑制病毒生长。这些数据表明，V蛋白的保守羧基末端在病毒生长中起重要作用。
Our previous results have shown that some residues of V protein-specific domain in human parainfluenza virus type 2 (hPIV2) are essential not only for STAT protein degradation but also for promoting virus growth. Here, we demonstrated that the virus growth of these recombinant hPIV2s (rPIV2) expressing mutated V proteins were improved in HeLa cell transiently expressing the wild-type V protein, but not in the cells constitutively expressing it. Consequently, we identified the region of the V protein that is essential for its oligomerization and for complex formation with NP protein. We also identified a host protein, AlP1/Alix, involved in apoptosis and efficient budding of several enveloped viruses as an interacting partner of the V and NP proteins. Depletion of AIP1/Alix by small interfering RNA suppressed virus growth. These data suggest that the conserved carboxyl terminus of the V protein plays an important role in virus growth.