Swine TRIM21 restricts FMDV infection via an intracellular neutralization mechanism

被引：40

作者：

Fan, Wenchun ^{[1
,2
]}

Zhang, Dong ^{[1
,2
]}

Qian, Ping ^{[1
,2
]}

Qian, Suhong ^{[1
,2
]}

Wu, Mengge ^{[1
,2
]}

Chen, Huanchun ^{[1
,2
]}

Li, Xiangmin ^{[1
,2
]}

机构：

[1] Huazhong Agr Univ, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China

[2] Huazhong Agr Univ, Div Anim Infect Dis, Coll Vet Med, 1 Shi Zi Shan St, Wuhan 430070, Peoples R China

来源：

ANTIVIRAL RESEARCH | 2016年 / 127卷

基金：

中国国家自然科学基金;

关键词：

Swine TRIM21; Foot-and-mouth disease virus; Antiviral activity; Antibodies; Neutralization; MOUTH-DISEASE VIRUS; FC-RECEPTOR TRIM21; I INTERFERON; ANTIVIRAL RESPONSE; FAMILY PROTEINS; E3; LIGASES; AAA-ATPASE; KAPPA-B; DEGRADATION; IMMUNITY;

D O I：

10.1016/j.antiviral.2016.01.004

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The tripartite motif protein 21 (TRIM21) is a ubiquitously expressed E3 ubiquitin ligase and an intracellular antibody receptor. TRIM21 mediates antibody-dependent intracellular neutralization (ADIN) in cytosol and provides an intracellular immune response to protect host defense against pathogen infection. In this study, swine TRIM21 (sTRIM21) was cloned and its role in ADIN was investigated. The expression of sTRIM21 is induced by type I interferon in PK-15 cells. sTRIM21 restricts FMDV infection in the presence of FMDV specific antibodies. Furthermore, sTRIM21 interacts with Fc fragment of swine immunoglobulin G (sFc) fused VP1 of FMDV and thereby causing its degradation. Both the RING and SPRY domains are essential for sTRIM21 to degrade sFc-fused VP1. These results suggest that the intracellular neutralization features of FMDV contribute to the antiviral activity of sTRIM21. sTRIM21 provide another intracellular mechanism to inhibit FMDV infection in infected cells. (C) 2016 Elsevier B.V. All rights reserved.

引用

页码：32 / 40

页数：9

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