1141-HBx与宿主蛋白Spindlin1的分子识别与转录调控机制

这份研究利用核磁共振（NMR）技术和AlphaFold模型，揭示了乙型肝炎病毒（HBV）中HBx蛋白及其致癌相关异构体HBx1-120的结构特性。研究发现，HBx1-120在游离状态下表现为本质无序蛋白，但在与宿主蛋白结合时会发生局部折叠。重点发现指出，HBx通过一种罕见的分子间锌指结构与表观遗传读取器Spindlin1形成强效的双价结合。这种结合机制能有效遮蔽Spindlin1的功能位点，阻止其与组蛋白尾部结合，进而干扰宿主对病毒DNA的转录控制。该发现不仅解析了HBx通过多价结合操控宿主防御系统的分子基础，也为理解HBV诱发肝细胞癌提供了新的结构视角。References:Clavier A, Shida T, Droemer MA, Gómez-Evain S, von Hammerstein F, Holzinger J, Leuthold MM, Douat C, Schütz AK. HBV HBx protein masks epigenetic reader Spindlin1 via an inter-molecular zinc finger to subvert transcriptional control. Nat Commun. 2026 May 25;17(1):4687. doi: 10.1038/s41467-026-72986-5. PMID: 42185260; PMCID: PMC13213052.前往小宇宙评论区与主播互动

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1141-HBx与宿主蛋白Spindlin1的分子识别与转录调控机制

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