病毒能够操纵宿主的泛素-蛋白酶体系统以利于自身的感染、致病。发现阻止病毒特异的泛素化过程的抑制剂是开发抗病毒药物的一种有效的途径。解析病毒和泛素-蛋白酶体系统在感染过程中的相互作用与调控机制是目前研究的热点之一。羊痘病毒与宿主泛素-蛋白酶体系统的相互作用尚未见实验报道。本项目以绵羊痘病毒（SPPV）140 RING finger蛋白为研究对象，采用体外泛素化检测技术、共聚焦显微技术、流式细胞术、Western blot等分子、生物化学方法，研究SPPV140的E3泛素连接酶活性；SPPV140与结合泛素的亚细胞定位；泛素化和蛋白酶体降解对SPPV140的调控作用。初步探讨SPPV140的泛素化相关功能，拓展对SPPV致病机理的认识，为研制抗痘病毒药物及其它相关研究提供技术平台和理论支撑。具有一定的科学意义及潜在的应用价值。

Virus can manipulate host ubiquitin-proteasome system to their own benefit, finding inhibitors that block a viral specific ubiquitylation process may be an effective approach for antiviral drug development. It is now a hot spot to decipher the regulation mechanism and interaction between virus and ubiquitin - proteasome system in the process of infection . The interaction between capripoxvirus and host ubiquitin-proteasome system remains to be established. In this project sheeppox virus 140 RING finger protein will be studied. Using vitro ubiquitination detection technology, confocal microscopy, flow cytometry, western blot and other molecular, biochemical methods, the E3 ubiquitin ligase activity of the SPPV140, the subcellular localization of the SPPV140 and conjugated ubiquitin,the regulatory role of ubiquitination and proteasomal degradation of SPPV140 will be investigate. Preliminary explore the ubiquitination related functions of SPPV140. These results will help us broaden our understanding of pathogenesis of sheep poxvirus, paving a way to develop drugs against sheeppox disease and providing technological platform for other related studies. Moreover, it has scientific and potential application implications.