Paramyxovirus Sendai virus-like particle formation by expression of multiple viral proteins and acceleration of its release by C protein.
Paramyxovirus Sendai virus-like particle formation by expression of multiple viral proteins and acceleration of its release by C protein.
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DOI：
10.1016/j.virol.2004.04.019
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发表时间：
2004-07
期刊：
影响因子：
3.7
通讯作者：
Fumihiro Sugahara;T. Uchiyama;Hitoshi Watanabe;Y. Shimazu;M. Kuwayama;Y. Fujii;K. Kiyotani;A. Adachi;N. Kohno;Tetsuya Yoshida;T. Sakaguchi
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文献类型：
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作者：
Fumihiro Sugahara;T. Uchiyama;Hitoshi Watanabe;Y. Shimazu;M. Kuwayama;Y. Fujii;K. Kiyotani;A. Adachi;N. Kohno;Tetsuya Yoshida;T. Sakaguchi
包膜病毒通过大分子组装和出芽成熟。为了研究这些步骤，我们产生了病毒样颗粒（VLP）的仙台病毒（SeV），一个原型的家庭副粘病毒科的结构蛋白的共表达。同时表达基质（M）、核-（N）、融合（F）和血凝素-神经氨酸酶（HN）蛋白导致产生具有与真实病毒颗粒相似的形态和密度的VLP，尽管从细胞释放的效率显著低于病毒。通过使用该VLP形成作为病毒出芽的模型，研究了单个蛋白质在出芽中的作用。M蛋白是出芽的驱动力，F蛋白促进VLP的释放，HN蛋白抑制VLP的释放。无论是糖蛋白，F或HN，以及N蛋白，VLP的密度显着转移到病毒颗粒的密度，表明病毒蛋白通过蛋白质-蛋白质相互作用带来的VLP的完整性。我们进一步发现，共表达的非结构蛋白，C，但不是V，增强VLP释放的水平，相当于病毒颗粒，表明C蛋白在病毒出芽中发挥作用。
Envelope viruses maturate by macromolecule assembly and budding. To investigate these steps, we generated virus-like particles (VLPs) by co-expression of structural proteins of Sendai virus (SeV), a prototype of the family Paramyxoviridae. Simultaneous expression of matrix (M), nucleo- (N), fusion (F), and hemagglutinin-neuraminidase (HN) proteins resulted in the generation of VLPs that had morphology and density similar to those of authentic virus particles, although the efficiency of release from cells was significantly lower than that of the virus. By using this VLP formation as a model of virus budding, roles of individual proteins in budding were investigated. The M protein was a driving force of budding, and the F protein facilitated and the HN protein suppressed VLP release. Either of the glycoproteins, F or HN, as well as the N protein, significantly shifted density of VLPs to that of virus particles, suggesting that viral proteins bring about integrity of VLPs by protein–protein interactions. We further found that co-expression of a nonstructural protein, C, but not V, enhanced VLP release to a level comparable to that of virus particles, demonstrating that the C protein plays a role in virus budding.