论文标题
干扰素诱导的跨膜蛋白3（IFITM3）及其抗病毒活性
Interferon-induced transmembrane protein 3 (IFITM3) and its antiviral activity
论文作者
论文摘要
包裹的病毒感染需要与细胞膜融合进行病毒基因组进入，仅在病毒和细胞膜相互作用后才发生以融合孔的形成，病毒访问细胞质。在这里，我们专注于干扰素诱导的跨膜蛋白3（IFITM3）及其抗病毒活性。 IFITM3预计将在中间状态阻塞或失速病毒融合，从而导致病毒传播失败。引入IFITM3后，我们描述了广义的脂质膜融合途径及其如何停滞，尤其是在IFITM3方面，以及有关IFITM3拓扑的当前问题。具体重点是抗病毒活性所必需的IFITM3两亲的A-螺旋（AAH）59V-68M。据报道，该肽的疏水性和疏水矩的计算以及来自其他膜重塑蛋白的活性位点肽。最后，我们讨论了翻译后修饰和定位的影响，IFITM3的AAH如何阻止病毒融合以及可能的后果。
Enveloped viral infections require fusion with cellular membranes for viral genome entry, occurring only following interaction of viral and cellular membranes allowing fusion pore formation, by which the virus accesses the cytoplasm. Here, we focus on interferon-induced transmembrane protein 3 (IFITM3) and its antiviral activity. IFITM3 is predicted to block or stall viral fusion at an intermediate state, causing viral propagation to fail. After introducing IFITM3, we describe the generalized lipid membrane fusion pathway and how it can be stalled, particularly with respect to IFITM3, and current questions regarding IFITM3's topology. Specific emphasis is placed on IFITM3's amphipathic a-helix (AAH) 59V-68M, necessary for antiviral activity. Calculations are reported of hydrophobicity and hydrophobic moment of this peptide and active site peptides from other membrane-remodeling proteins. Finally, we discuss the effects of post-translational modifications and localization, how IFITM3's AAH may block viral fusion, and possible ramifications of membrane composition.
