Cholesterol 25-hydroxylase inhibits Senecavirus A replication by enzyme activity-dependent and independent mechanisms

被引：5
|
作者：
Zhu, Huixin [1 ]
Yan, Junfang [1 ]
Liu, Xing [1 ,2 ]
Li, Liang [1 ]
Liu, Wenwen [1 ]
Wang, Xianwei [1 ,2 ]
Jiang, Ping [1 ,2 ]
Bai, Juan [1 ,2 ]
机构：
[1] Nanjing Agr Univ, Coll Vet Med, Key Lab Anim Dis Diagnost & Immunol,Minist Agr, MOE Int Joint Collaborat Res Lab Anim Hlth & Food, Nanjing 210095, Peoples R China
[2] Yangzhou Univ, Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou 225009, Jiangsu, Peoples R China
来源：
VETERINARY MICROBIOLOGY | 2021年 / 256卷
关键词：
CH25H; 25HC; SVA infection; Degradation; 3A protein; HOST RESTRICTION FACTOR; VESICULAR DISEASE; SWINE;
D O I：
10.1016/j.vetmic.2021.109038
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Cholesterol 25-hydroxylase (CH25 H), as a host restriction factor, has been reported to take a broad-spectrum antiviral effect. However, the role of CH25H in Senecavirus A (SVA) infection remains unknown. In this study, we first demonstrate that overexpression of CH25H inhibits SVA replication. Consistently, knockdown or knockout of the endogens CH25H promotes SVA infection. Further, the anti-SVA effect of 25-hydroxycholesterol (25HC), which is the product of CH25H, operates via inhibition of viral attachment and replication. On the other hand, the CH25H mutant (CH25H-M) lacking hydroxylase activity still restricts SVA infection, which can selectively interact and degrade SVA 3A protein via the ubiquitin-proteasome manner. Altogether, these results suggest that CH25H has an antiviral function in SVA infection and provides an alternative manner to control SVA.
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