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棉铃虫单核衣壳核多角体病毒的F蛋白可被甜菜夜蛾多核衣壳核多角体病毒的同源物功能性替代。

The F protein of Helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from Spodoptera exigua multiple nucleopolyhedrovirus.

作者信息

Wang Manli, Tan Ying, Yin Feifei, Deng Fei, Vlak Just M, Hu Zhihong, Wang Hualin

机构信息

Graduate School of the Chinese Academy of Sciences, Beijing 100039, PR China.

State Key Laboratory of Virology and Joint Laboratory of Invertebrate Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, PR China.

出版信息

J Gen Virol. 2008 Mar;89(Pt 3):791-798. doi: 10.1099/vir.0.83466-0.

Abstract

F proteins of group II nucleopolyhedroviruses (NPVs) are envelope fusion proteins essential for virus entry and egress. An F-null Helicoverpa armigera single nucleocapsid NPV (HearNPV) bacmid, HaBacDeltaF, was constructed. This bacmid could not produce infectious budded virus (BV) when transfected into HzAM1 cells, showing that F protein is essential for cell-to-cell transmission of BVs. When HaBacDeltaF was pseudotyped with the homologous F protein (HaBacDeltaF-HaF, positive control) or with the heterologous F protein from Spodoptera exigua multinucleocapsid NPV (SeMNPV) (HaBacDeltaF-SeF), infectious BVs were produced with similar kinetics. In the late phase of infection, the BV titre of HaBacDeltaF-SeF virus was about ten times lower than that of HaBacDeltaF-HaF virus. Both pseudotyped viruses were able to fuse HzAM1 cells in a similar fashion. The F proteins of both HearNPV and SeMNPV were completely cleaved into F(1) and F(2) in the BVs of vHaBacDeltaF-HaF and vHaBacDeltaF-SeF, respectively, but the cleavage of SeF in vHaBacDeltaF-SeF-infected HzAM1 cells was incomplete, explaining the lower BV titre of vHaBacDeltaF-SeF. Polyclonal antisera against HaF(1) and SeF(1) specifically neutralized the infection of vHaBacDeltaF-HaF and vHaBacDeltaF-SeF, respectively. HaF(1) antiserum showed some cross-neutralization with vHaBacDeltaF-SeF. These results demonstrate that group II NPV F proteins can be functionally replaced with a homologue of other group II NPVs, suggesting that the interaction of F with other viral or host proteins is not absolutely species-specific.

摘要

II 组核多角体病毒(NPV)的 F 蛋白是病毒进入和释放所必需的包膜融合蛋白。构建了一个缺失 F 蛋白的棉铃虫单粒包埋核多角体病毒(HearNPV)杆粒,即 HaBacDeltaF。将该杆粒转染到 HzAM1 细胞中时不能产生感染性出芽病毒(BV),这表明 F 蛋白对于 BV 的细胞间传播至关重要。当 HaBacDeltaF 用同源 F 蛋白(HaBacDeltaF-HaF,阳性对照)或来自甜菜夜蛾多粒包埋核多角体病毒(SeMNPV)的异源 F 蛋白(HaBacDeltaF-SeF)进行假型化时,能产生具有相似动力学的感染性 BV。在感染后期,HaBacDeltaF-SeF 病毒的 BV 滴度比 HaBacDeltaF-HaF 病毒低约十倍。两种假型化病毒都能以相似的方式融合 HzAM1 细胞。在 vHaBacDeltaF-HaF 和 vHaBacDeltaF-SeF 的 BV 中,HearNPV 和 SeMNPV 的 F 蛋白分别完全裂解为 F(1)和 F(2),但在 vHaBacDeltaF-SeF 感染的 HzAM1 细胞中 SeF 的裂解不完全,这解释了 vHaBacDeltaF-SeF 的 BV 滴度较低的原因。针对 HaF(1)和 SeF(1)的多克隆抗血清分别特异性中和了 vHaBacDeltaF-HaF 和 vHaBacDeltaF-SeF 的感染。HaF(1)抗血清对 vHaBacDeltaF-SeF 表现出一定的交叉中和作用。这些结果表明,II 组 NPV 的 F 蛋白可以被其他 II 组 NPV 的同源物功能性替代,这表明 F 与其他病毒或宿主蛋白的相互作用并非绝对具有物种特异性。

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