School of Plant and Environmental Sciences, Virginia Tech, Blacksburg, Virginia, United States of America.
Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Key Lab of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Nanjing, China.
PLoS Pathog. 2022 Sep 1;18(9):e1010752. doi: 10.1371/journal.ppat.1010752. eCollection 2022 Sep.
Positive-strand RNA viruses assemble their viral replication complexes (VRCs) on specific host organelle membranes, yet it is unclear how viral replication proteins recognize and what motifs or domains in viral replication proteins determine their destinations. We show here that an amphipathic helix, helix B in replication protein 1a of brome mosaic virus (BMV), is necessary for 1a's localization to the nuclear endoplasmic reticulum (ER) membrane where BMV assembles its VRCs. Helix B is also sufficient to target soluble proteins to the nuclear ER membrane in yeast and plant cells. We further show that an equivalent helix in several plant- and human-infecting viruses of the Alsuviricetes class targets fluorescent proteins to the organelle membranes where they form their VRCs, including ER, vacuole, and Golgi membranes. Our work reveals a conserved helix that governs the localization of VRCs among a group of viruses and points to a possible target for developing broad-spectrum antiviral strategies.
正链 RNA 病毒在特定的宿主细胞器膜上组装它们的病毒复制复合物（VRC），但尚不清楚病毒复制蛋白如何识别以及病毒复制蛋白中的哪些模体或结构域决定它们的靶位。我们在这里表明，雀麦花叶病毒（BMV）复制蛋白 1a 中的一个两亲性螺旋，即螺旋 B，对于 1a 定位于核内质网（ER）膜是必需的，BMV 在那里组装其 VRC。螺旋 B 也足以将可溶性蛋白靶向酵母和植物细胞的核 ER 膜。我们进一步表明，Alsuviricetes 类的几种感染植物和人类的病毒中的等效螺旋将荧光蛋白靶向形成 VRC 的细胞器膜，包括 ER、液泡和高尔基体膜。我们的工作揭示了一种保守的螺旋，它控制着一组病毒中 VRC 的定位，并指出了开发广谱抗病毒策略的可能靶标。
