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Inhibition of Antiviral Innate Immunity by Foot-and-Mouth Disease Virus L-pro through Interaction with the N-Terminal Domain of Swine RNase L

文献类型： 外文期刊

作者： Sui, Chao 1 ; Jiang, Dandan 1 ; Wu, Xiangju 1 ; Liu, Sidang 2 ; Li, Feng 3 ; Pan, Li 5 ; Cong, Xiaoyan 1 ; Li, Juntong 1 ; Y 1 ;

作者机构： 1.Shandong Acad Agr Sci, Inst Anim Sci & Vet Med, Shandong Key Lab Anim Dis Control & Breeding, Jinan, Shandong, Peoples R China

2.Shandong Agr Univ, Coll Anim Sci & Technol, Shandong Prov Key Lab Anim Biotechnol & Dis Contr, Tai An, Shandong, Peoples R China

3.South Dakota State Univ, Dept Biol & Microbiol, Brookings, SD 57007 USA

4.South Dakota State Univ, Dept Vet & Biomed Sci, Brookings, SD 57007 USA

5.Chinese Acad Agr Sci, Lanzhou Vet Res Inst, State Key Lab Vet Etiol Biol,Minist Agr, Natl Foot & Mouth Dis Reference Lab,Key Lab Anim, Lanzhou, Gansu, Peoples R China

6.Univ Illinois, Dept Pathobiol, Urbana, IL USA

7.ARS, Virus & Prion Res Unit, Natl Anim Dis Ctr, USDA, Ames, IA USA

8.Kyungpook Natl Univ, Sch Life Sci, Anim Virol Lab, BK21 Plus KNU Creat BioRes Grp, Daegu, South Korea

关键词： FMDV; RNase L; L-pro; antagonistic mechanism; ISGs; foot-and-mouth disease virus

期刊名称：JOURNAL OF VIROLOGY （ 影响因子：5.103； 五年影响因子：5.078 ）

ISSN： 0022-538X

年卷期： 2021 年 95 卷 15 期

页码：

收录情况： SCI

摘要： Foot-and-mouth disease virus (FMDV) is the pathogen of foot-and-mouth disease (FMD), which is a highly contagious disease in cloven-hoofed animals. To survive in the host, FMDV has evolved multiple strategies to antagonize host innate immune responses. In this study, we showed that the leader protease (Lpro) of FMDV, a papain-like proteinase, promoted viral replication by evading the antiviral interferon response through counteracting the 2',5'-oligoadenylate synthetase (OAS)/RNase L system. Specifically, we observed that the titers of Lpro deletion virus were significantly lower than those of wild type FMDV (FMDV-WT) in cultured cells. Our mechanistic studies demonstrated that Lpro interfered with the OAS/RNase L pathway by interacting with the N-terminal domain of swine RNase L (sRNase L). Remarkably, Lpro of FMDV exhibited species-specific binding to RNase L in that the interaction was observed only in swine cells, not human, monkey, or canine cells. Lastly, we presented evidence that by interacting with sRNase L, FMDV Lpro inhibited cellular apoptosis. Taken together, these results demonstrate a novel mechanism that Lpro utilizes to escape the OAS/RNase L-mediated antiviral defense pathway. IMPORTANCE FMDV is a picornavirus that causes a significant disease in agricultural animals. FMDV has developed diverse strategies to escape the host interferon response. Here, we show that Lpro of FMDV antagonizes the OAS/RNase L pathway, an important interferon effector pathway, by interacting with the N-terminal domain of sRNase L. Interestingly, such a virus-host interaction is species-specific because the interaction is detected only in swine cells, not in human, monkey, or canine cells. Furthermore, Lpro inhibits apoptosis through interacting with sRNase L. This study demonstrates a novel mechanism by which FMDV has evolved to inhibit host innate immune responses.

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