A conserved viral amphipathic helix governs the replication site-specific membrane association
文献类型： 外文期刊
作者： Sathanantham, Preethi 1 ; Zhao, Wenhao 1 ; He, Guijuan 1 ; Murray, Austin 1 ; Fenech, Emma 3 ; Diaz, Arturo 4 ; Schuldiner, Maya 3 ; Wang, Xiaofeng 1 ;
作者机构： 1.Virginia Tech, Sch Plant & Environm Sci, Blacksburg, VA 24061 USA
2.Jiangsu Acad Agr Sci, Inst Plant Protect, Key Lab Food Qual & Safety Jiangsu Prov, State Key Lab Breeding Base, Nanjing, Peoples R China
3.Weizmann Inst Sci, Dept Mol Genet, Rehovot, Israel
4.La Sierra Univ, Dept Biol, Riverside, CA USA
期刊名称：PLOS PATHOGENS （ 影响因子：7.464； 五年影响因子：7.913 ）
ISSN： 1553-7366
年卷期： 2022 年 18 卷 9 期
页码：
收录情况： SCI
摘要： 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 1 a of brome mosaic virus (BMV), is necessary for la'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.
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