Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, China.
Viruses. 2020 Dec 27;13(1):31. doi: 10.3390/v13010031.
Membrane proteins of enveloped viruses have been reported to undergo palmitoylation, a post-translational modification often having a critical role in the function of these viral proteins and hence viral replication. In this study, we report that the foamy virus (FV) envelope (Env) glycoprotein is palmitoylated. Specifically, we found that bovine foamy virus (BFV) Env (BEnv) is palmitoylated at amino acid positions C58 and C59 by BDHHC3 and BDHHC20 in a DHHC motif-dependent manner. In addition, mutations C58S and C58/59S significantly decrease cell surface expression of BEnv, subviral particle (SVP) egress, and its membrane fusion activity, thus ultimately inhibiting BFV replication. The C59S mutation exerts a minor effect in this regard. Taken together, these data demonstrate that the function of BEnv in the context of BFV replication is under the regulation of palmitoylation.
包膜病毒的膜蛋白已被报道发生棕榈酰化，这是一种翻译后修饰，通常在这些病毒蛋白的功能和病毒复制中起关键作用。在这项研究中，我们报告称泡沫病毒（FV）包膜（Env）糖蛋白发生棕榈酰化。具体而言，我们发现牛泡沫病毒（BFV）Env（BEnv）通过 DHHC 基序依赖的方式被 BDHHC3 和 BDHHC20 棕榈酰化在氨基酸位置 C58 和 C59 处。此外，突变 C58S 和 C58/59S 显著降低 BEnv 的细胞表面表达、亚病毒颗粒（SVP）出芽和其膜融合活性，从而最终抑制 BFV 复制。C59S 突变在此方面的影响较小。总之，这些数据表明，BFV 复制背景下 BEnv 的功能受棕榈酰化调节。
