Selected article for: "broad spectrum and host host"
Author: Yuan, Shuofeng; Chu, Hin; Chan, Jasper Fuk-Woo; Ye, Zi-Wei; Wen, Lei; Yan, Bingpeng; Lai, Pok-Man; Tee, Kah-Meng; Huang, Jingjing; Chen, Dongdong; Li, Cun; Zhao, Xiaoyu; Yang, Dong; Chiu, Man Chun; Yip, Cyril; Poon, Vincent Kwok-Man; Chan, Chris Chung-Sing; Sze, Kong-Hung; Zhou, Jie; Chan, Ivy Hau-Yee; Kok, Kin-Hang; To, Kelvin Kai-Wang; Kao, Richard Yi-Tsun; Lau, Johnson Yiu-Nam; Jin, Dong-Yan; Perlman, Stanley; Yuen, Kwok-Yung
Title: SREBP-dependent lipidomic reprogramming as a broad-spectrum antiviral target
  • Cord-id: m7toy4j0
  • Document date: 2019_1_10
    • ID: m7toy4j0
    Snippet: Viruses are obligate intracellular microbes that exploit the host metabolic machineries to meet their biosynthetic demands, making these host pathways potential therapeutic targets. Here, by exploring a lipid library, we show that AM580, a retinoid derivative and RAR-α agonist, is highly potent in interrupting the life cycle of diverse viruses including Middle East respiratory syndrome coronavirus and influenza A virus. Using click chemistry, the overexpressed sterol regulatory element binding
    Document: Viruses are obligate intracellular microbes that exploit the host metabolic machineries to meet their biosynthetic demands, making these host pathways potential therapeutic targets. Here, by exploring a lipid library, we show that AM580, a retinoid derivative and RAR-α agonist, is highly potent in interrupting the life cycle of diverse viruses including Middle East respiratory syndrome coronavirus and influenza A virus. Using click chemistry, the overexpressed sterol regulatory element binding protein (SREBP) is shown to interact with AM580, which accounts for its broad-spectrum antiviral activity. Mechanistic studies pinpoint multiple SREBP proteolytic processes and SREBP-regulated lipid biosynthesis pathways, including the downstream viral protein palmitoylation and double-membrane vesicles formation, that are indispensable for virus replication. Collectively, our study identifies a basic lipogenic transactivation event with broad relevance to human viral infections and represents SREBP as a potential target for the development of broad-spectrum antiviral strategies.

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