State Key Laboratory of Crop Stress Biology for Arid Areas, Key Laboratory of Integrated Pest Management on Crops in Northwestern Loess Plateau, Ministry of Agriculture, College of Plant Protection, Northwest A&F University, Yangling, Shaanxi, 712100, China.
State Key Laboratory of Crop Stress Biology for Arid Areas, Key Laboratory of Integrated Pest Management on Crops in Northwestern Loess Plateau, Ministry of Agriculture, College of Plant Protection, Northwest A&F University, Yangling, Shaanxi, 712100, China.
Virology. 2020 Feb;541:85-100. doi: 10.1016/j.virol.2019.12.003. Epub 2019 Dec 12.
The endosomal sorting complex required for transport (ESCRT) pathway is required for efficient egress of Autographa californica multiple nucleopolyhedrovirus (AcMNPV). In this study, we found that Ac93, a baculovirus core protein, contains a conserved MIM1-like motif. Alanine substitutions for six leucine residues in MIM1-like motif revealed that L142, L145, L146, and L149 are required for association of Ac93 with the MIT domain of Vps4. Mutations of these residues also blocked self-association and the association of Ac93 with ESCRT-III proteins or other viral core proteins Ac76 and Ac103, and resulted in a substantial reduction of infectious virus production, less efficient nuclear egress of progeny nucleocapsids, and the defect of intranuclear microvesicles formation. Combined with the localization of the association of Ac93 with ESCRT-III/Vps4 and other viral proteins at the nuclear membrane, we propose that the coordinated action of these viral proteins and ESCRT-III/Vps4 may be involved in remodeling the nuclear membrane.
内体分选复合物需要运输（ESCRT）途径是有效的蛾多角体病毒（AcMNPV）退出所必需的。在这项研究中，我们发现 Ac93，一种杆状病毒核心蛋白，含有一个保守的 MIM1 样基序。在 MIM1 样基序中的六个亮氨酸残基的丙氨酸取代表明 L142、L145、L146 和 L149 对于 Ac93 与 Vps4 的 MIT 结构域的关联是必需的。这些残基的突变也阻断了自身关联以及 Ac93 与 ESCRT-III 蛋白或其他病毒核心蛋白 Ac76 和 Ac103 的关联，并导致感染性病毒产量的大量减少，后代核衣壳更有效地核出芽，以及核内微泡形成的缺陷。结合 Ac93 与 ESCRT-III/Vps4 和其他病毒蛋白在核膜上的关联定位，我们提出这些病毒蛋白和 ESCRT-III/Vps4 的协调作用可能参与重塑核膜。
