文献类型： 外文期刊
作者： Yang, Jingjing 1 ; Li, Zijian 1 ; Ma, Ruiyi 3 ; Xie, Shijie 3 ; Wang, Dan 3 ; Quan, Rong 3 ; Wen, Xuexia 1 ; Song, Jiangwei 3 ;
作者机构： 1.Shenyang Agr Univ, Coll Anim Sci & Vet Med, Key Lab Livestock Infect Dis, Minist Educ, 120 Dongling Rd, Shenyang 110866, Peoples R China
2.Shenyang Agr Univ, Coll Anim Sci & Vet Med, Key Lab Ruminant Infect Dis Prevent & Control East, Minist Agr & Rural Affairs, 120 Dongling Rd, Shenyang 110866, Peoples R China
3.Beijing Acad Agr & Forestry Sci, Inst Anim Husb & Vet Med, Beijing Key Lab Prevent & Control Infect Dis Lives, 9 Shuguang Garden Middle Rd, Beijing 100097, Peoples R China
关键词： Seneca Valley virus (SVV); DCP1A; 3C protease; 3D; cleavage
期刊名称：VETERINARY RESEARCH （ 影响因子：3.5； 五年影响因子：4.0 ）
ISSN： 0928-4249
年卷期： 2025 年 56 卷 1 期
页码：
收录情况： SCI
摘要： Seneca Valley virus (SVV), a new member of Picornaviridae, causes idiopathic vesicular symptoms in pregnant sows and acute death in neonatal piglets, considerably damaging the swine industry. The viral protease 3C (3Cpro) cleaves host immune-related molecules to create a favorable environment for viral replication. In this study, we found that mRNA decapping enzyme 1A (DCP1A) is a novel antiviral effector against SVV infection that targets 3D viral RNA-dependent RNA polymerase for OPTN-mediated autophagic degradation. To counteract this effect, SVV 3Cpro targets DCP1A for cleavage at glutamine 343 (Q343), resulting in the cleaved products DCP1A (1-343) and DCP1A (344-580), which lose the ability to restrict SVV replication. In contrast, the 3C cleavage-resistant DCP1A-Q343A mutant exhibited stronger antiviral effects than the wild-type DCP1A. Additionally, the degradation of the viral 3D protein targeted by DCP1A was abolished after its cleavage by SVV 3Cpro. In conclusion, our study demonstrated that SVV 3Cpro is a pivotal ISG antagonist that cleaves DCP1A. These results offer novel insight into how viruses evade host immunity.
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