Inhibition of Cavin3 Degradation by the Human Parainfluenza Virus Type 2 V Protein Is Important for Efficient Viral Growth
Inhibition of Cavin3 Degradation by the Human Parainfluenza Virus Type 2 V Protein Is Important for Efficient Viral Growth
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DOI：
10.3389/fmicb.2020.00803
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发表时间：
2020-04
影响因子：
5.2
通讯作者：
K. Ohta;Yusuke Matsumoto;M. Nishio
中科院分区：
文献类型：
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作者：
K. Ohta;Yusuke Matsumoto;M. Nishio
Cavin蛋白在脂筏微区小窝的形成中起重要作用。用人副流感病毒2型（hPIV-2）感染的细胞的脉冲追踪实验显示Cavin 3的蛋白酶体降解减少。单独过表达hPIV-2 V蛋白足以抑制Cavin 3降解。免疫沉淀分析显示V蛋白与Cavin 3结合。V蛋白的C-末端区域内的Trp残基以及Cavin 3的N-末端区域内的Trp残基对于V-Cavin 3相互作用是重要的。Cavin 3敲低抑制hPIV-2生长，而不影响其进入、复制、转录或翻译。在V蛋白过表达的细胞中观察到比在脂筏微区中的对照细胞中更高量的Cavin 3。我们的数据共同表明，hPIV-2 V蛋白结合并稳定Cavin 3，这反过来又促进了组装和出芽的hPIV-2在脂筏微结构域。
Cavin proteins have important roles in the formation of caveolae in lipid raft microdomains. Pulse-chase experiments of cells infected with human parainfluenza virus type 2 (hPIV-2) showed decreased proteasomal degradation of Cavin3. Overexpression of hPIV-2 V protein alone was sufficient to inhibit Cavin3 degradation. Immunoprecipitation analysis revealed that V protein bound to Cavin3. Trp residues within C-terminal region of V protein, as well as the N-terminal region of Cavin3, are important for V–Cavin3 interaction. Cavin3 knockdown suppressed hPIV-2 growth without affecting its entry, replication, transcription, or translation. Higher amounts of Cavin3 were observed in V protein-overexpressing cells than in control cells in lipid raft microdomains. Our data collectively suggest that hPIV-2 V protein binds to and stabilizes Cavin3, which in turn facilitates assembly and budding of hPIV-2 in lipid raft microdomains.