![]() Received: DecemAccepted: JPublished: September 1, 2022Ĭopyright: © 2022 Sathanantham et al. (2022) A conserved viral amphipathic helix governs the replication site-specific membrane association. Our results reveal a conserved feature among a group of viruses in governing the associations with replication site-specific organelle membranes and point to a target to develop broad-spectrum antivirals.Ĭitation: Sathanantham P, Zhao W, He G, Murray A, Fenech E, Diaz A, et al. We further show that the helix B across members of the Alsuviricetes class is sufficient to target fluorescence proteins to the designated organelle membranes. BMV belongs to the Alsuviricetes class that includes viruses infecting humans, animals, and plants. In addition, Helix B is sufficient to target several soluble proteins to the nuclear ER membrane in yeast and plant cells. We show that an amphipathic alpha-helix, helix B, in BMV 1a is necessary for the association of BMV 1a with the nuclear ER membrane and for BMV genome amplification. For brome mosaic virus (BMV), its replication protein 1a is responsible for the VRC formation at the nuclear endoplasmic reticulum (ER) membrane. An initial step to form VRCs is to target viral replication proteins to the designated organelle membranes. During their infections, (+)RNA viruses assemble their viral replication complexes (VRCs), where they multiply themselves, at specific organelle membranes. Positive-strand RNA viruses are the largest viral class that include numerous pathogens causing important diseases in humans, animals, and plants. 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. 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. Helix B is also sufficient to target soluble proteins to the nuclear ER membrane in yeast and plant cells. ![]() 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. 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. ![]()
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