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SREBP-dependent Lipidomic Reprogramming as a Broad-Spectrum Antiviral Target

SREBP-dependent Lipidomic Reprogramming as a Broad-Spectrum Antiviral Target

Shuofeng Yuan, Hin Chu, Jasper Fuk-Woo Chan, Zi-Wei Ye, Lei Wen, Bingpeng Yan, Pok-Man Lai, Kah-Meng Tee, Jingjing Huang, Dongdong Chen, Cun Li, Xiaoyu Zhao, Dong Yang, Man Chun Chiu, Cyril Yip, Vincent Kwok-Man Poon, etc.

Nat Commun. 2019 Jan 10;10(1):120.

PMID: 30631056

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP102121608	AM580		102121-60-8	Price

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