脂酰化是一种重要的蛋白翻译后修饰，主要包括棕榈酰化、豆蔻酰化、异戊烯化和糖基化磷脂酰肌醇（GPI）共价结合4种方式。不同的病毒蛋白可发生不同类型的脂酰化，其生物学功能也会发生相应改变。棕榈酰化通常能增强病毒跨膜蛋白的疏水性，调节这些蛋白的胞内运输及定位，进一步影响病毒感染过程中的膜融合、病毒颗粒装配及释放等步骤。豆蔻酰化则可调控病毒蛋白表面的正电荷强度，使病毒蛋白与脂质膜的亲和力改变，如preS1豆蔻酰化加强乙型肝炎病毒（HBV）和丁型肝炎病毒（HDV）的受体识别能力和感染性，而人类免疫缺陷病毒（HIV）Nef豆蔻酰化为病毒调节感染及免疫应答所必需。异戊烯化能使病毒游离的蛋白与膜结合，并介导蛋白间的相互作用，如L-HDAg异戊烯化有利于其运输至内质网膜上，与HBV表面抗原（HBsAg）及HDV RNA共同形成HDV颗粒。此外，一些病毒蛋白与GPI通过共价结合形成复合物，GPI基团可改变感染细胞的膜结构及胞质内磷脂构成，如GPI与朊蛋白（PrP）结合导致细胞朊蛋白（PrP^c）交联或羊瘙痒病朊蛋白（PrP^sc）聚集，与朊病毒引起的海绵样病变有关。对病毒蛋白脂酰化机制进一步了解，有利于设计和开发以此为靶点的特异性抗病毒新药。

Fatty acylation, a posttranslational modification of proteins, is classified into four fundamental forms：palmitoylation, myristoylation, prenylation, and the covalent binding of glycosylphosphatidylinositol (GPI). All forms of fatty acylation may occur on the proteins from a variety of viruses. And the modified proteins are consequently altered in functions. Palmitoylation regulates the intercellular transportation and location of viral transmembrane proteins via enhancing the hydrophobicity, which is involved in the membrane fusion, assembly, and release during virus infection and replication. Through the regulation of the positive charges of protein’s surfaces, myristoylation changes the affinity between the cellular membrane and some viral proteins, for example, the modification of preS1 increases the receptor recognition and infectivity of both hepatitis B virus (HBV) and hepatitis D virus (HDV), and the myristoylation of Nef is necessary for regulation of human immunodeficiency virus (HIV) infection and immunity. The interaction of viral free proteins with the membrane compartments or other proteins is increased after prenylation. For example, prenylation could facilitate L-HDAg’s trafficking to endoplasmic reticulum, in which the proteins are assembled into HDV virions together with HBV surface antigen (HBsAg) and HDV RNA . Additionally, GPI binds to viral proteins covalently, and the GPI moiety would change the membrane structure or cytoplasmic phospholipid components of infected cells. For example, GPI modification induced the cross-linkage of cellular prion protein (PrP^C) and agglutination of scrapie prion protein (PrP^SC), which is involved in the spongiform pathogenesis induced by the prions. It would be greatly beneficial for both design and development of new antiviral drugs when the mechanism of lipid modification of viral proteins is further uncovered.