The entry of enveloped virus requires the fusion of viral and host cell membranes. An effective fusion inhibitor aiming at impeding such membrane fusion may emerge as a broad‐spectrum antiviral agent against a wide range of viral infections. Mycobacterium survives inside the phagosome by inhibiting phagosome–lysosome fusion with the help of a coat protein coronin 1. Structural analysis of coronin 1 and other WD40‐repeat protein suggest that the trp‐asp (WD) sequence is placed at distorted β‐meander motif (more exposed) in coronin 1. The unique structural feature of coronin 1 was explored to identify a simple lipo‐peptide sequence (myr‐WD), which effectively inhibits membrane fusion by modulating the interfacial order, water penetration, and surface potential. The mycobacterium inspired lipo‐dipeptide was successfully tested to combat type 1 influenza virus (H1N1) and murine coronavirus infections as a potential broad‐spectrum antiviral agent.

中文翻译：

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转化分枝杆菌生存策略以开发基于脂肽的融合抑制剂**

有包膜病毒的进入需要病毒与宿主细胞膜的融合。旨在阻止这种膜融合的有效融合抑制剂可能会成为针对多种病毒感染的广谱抗病毒剂。分枝杆菌通过外壳蛋白 Coronin 1 抑制吞噬体-溶酶体融合而在吞噬体内存活。Coronin 1 和其他 WD40 重复蛋白的结构分析表明，trp-asp (WD) 序列位于扭曲的 β-meander 基序上Coronin 1 中的（更多暴露）。探索了 Coronin 1 的独特结构特征，以确定一个简单的脂肽序列 (myr-WD)，它通过调节界面顺序、水渗透和表面电位来有效抑制膜融合。分枝杆菌启发的脂二肽作为潜在的广谱抗病毒剂已成功测试可对抗 1 型流感病毒 (H1N1) 和鼠冠状病毒感染。