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
摘要：
包膜病毒感染需要与细胞膜融合以进入病毒基因组，仅在病毒和细胞膜相互作用后发生，允许融合孔形成，病毒通过融合孔进入细胞质。在这里，我们专注于干扰素诱导的跨膜蛋白3（IFITM 3）及其抗病毒活性。预计IFITM 3在中间状态阻断或停止病毒融合，导致病毒繁殖失败。在介绍IFITM 3后，我们描述了广义的脂质膜融合途径，以及它是如何被阻止的，特别是关于IFITM 3，以及关于IFITM 3拓扑结构的当前问题。特别强调IFITM 3的两亲性α-螺旋（AAH）59 V-68 M，这是抗病毒活性所必需的。计算了该肽和其他膜重塑蛋白活性位点肽的疏水性和疏水矩。最后，我们讨论了翻译后修饰和定位的影响，IFITM 3的AAH如何可能阻止病毒融合，以及膜组成的可能后果。
英文摘要：
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.
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