翻译：翻译：翻译：翻译：翻译：翻译：翻译：翻译：翻译： 后翻译修饰（PTMs）对于宿主抗病毒免疫应答和病毒免疫逃逸至关重要。在一组新型酰基化反应中，已经检测到赖氨酸丙酰化（Kpr）存在于组蛋白和非组蛋白蛋白中。然而，是否存在任何病毒蛋白中的蛋白丙酰化以及这些修饰是否调节病毒免疫逃逸仍然是未知的。 在这里，我们展示了卡波西肉瘤相关疱疹病毒（KSHV）编码的病毒干扰素调节因子1（vIRF1）可以在赖氨酸残基中丙酰化，这对于有效抑制IFN-β的产生和抗病毒信号传导是必需的。从机械上讲，vIRF1通过阻塞SIRT6与泛素特异性蛋白酶10（USP10）的相互作用，从而促进自身的丙酰化，并通过泛素蛋白酶途径降解USP10。此外，vIRF1的丙酰化对于其阻断IRF3-CBP / p300的招募和压制STING DNA感测通路的功能是必需的。 SIRT6特异性激活剂UBCS039可以拯救丙酰化vIRF1介导的IFN-β信号通路的抑制。这些结果揭示了一种通过病毒蛋白的丙酰化机制逃避先天免疫的新机制。这些发现表明，参与病毒丙酰化的酶可能是预防病毒感染的潜在靶点。 版权：© 2023 Shi等。这是一篇根据创作公共许可证分发的开放获取文章，允许在任何媒介上进行无限制的使用，分发和复制，前提是原作者和来源得到了资格的认可。

Post-translational modifications (PTMs) are essential for host antiviral immune response and viral immune evasion. Among a set of novel acylations, lysine propionylation (Kpr) has been detected in both histone and non-histone proteins. However, whether protein propionylation occurs in any viral proteins and whether such modifications regulate viral immune evasion remain elusive. Here, we show that Kaposi's sarcoma-associated herpesvirus (KSHV)-encoded viral interferon regulatory factor 1 (vIRF1) can be propionylated in lysine residues, which is required for effective inhibition of IFN-β production and antiviral signaling. Mechanistically, vIRF1 promotes its own propionylation by blocking SIRT6's interaction with ubiquitin-specific peptidase 10 (USP10) leading to its degradation via a ubiquitin-proteasome pathway. Furthermore, vIRF1 propionylation is required for its function to block IRF3-CBP/p300 recruitment and repress the STING DNA sensing pathway. A SIRT6-specific activator, UBCS039, rescues propionylated vIRF1-mediated repression of IFN-β signaling. These results reveal a novel mechanism of viral evasion of innate immunity through propionylation of a viral protein. The findings suggest that enzymes involved in viral propionylation could be potential targets for preventing viral infections.Copyright: © 2023 Shi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.