MARCH1 and MARCH2 inhibit pseudorabies virus replication by trapping the viral cell-to-cell fusion complex in trans-Golgi network
文献类型: 外文期刊
第一作者: Huang, Rui
作者: Huang, Rui;Rao, Cui-Hong;Bai, Yuan-Zhe;Chen, Meng;Peng, Jin-Mei;Xu, Shi-Jia;Sun, Yue;Fandan, Meng;Khan, Mirwaise;An, Tong-Qing;Tian, Zhi-Jun;Cai, Xue-Hui;Tang, Yan-Dong;Huang, Rui;Wang, Gang;Yu, Changqing;Chen, Meng;Cai, Xue-Hui;Tang, Yan-Dong;Chen, Meng;Tang, Yan-Dong;Lyu, Chuang
作者机构:
关键词: MARCH1; MARCH2; Pseudorabies virus; Herpesvirus; Cell-to-cell fusion; Glycoprotein B; Furin
期刊名称:VETERINARY MICROBIOLOGY ( 影响因子:2.4; 五年影响因子:2.6 )
ISSN: 0378-1135
年卷期: 2024 年 295 卷
页码:
收录情况: SCI
摘要: The membrane-associated RING-CH (MARCH) family of proteins are members of the E3 ubiquitin ligase family and are essential for a variety of biological functions. Currently, MARCH proteins are discovered to execute antiviral functions by directly triggering viral protein degradation or blocking the furin cleavage of viral class I fusion proteins. Here, we report a novel antiviral mechanism of MARCH1 and MARCH2 (MARCH1/2) in the replication of Pseudorabies virus (PRV), a member of the Herpesviridae family. We discovered MARCH1/2 restrict PRV replication at the cell-to-cell fusion step. Furthermore, MARCH1/2 block gB cleavage, and this is dependent on their E3 ligase activity. Interestingly, the blocking of gB cleavage by MARCH1/2 does not contribute to their antiviral activity in vitro. We discovered that MARCH1/2 are associated with the cell-to-cell fusion complex of gB, gD, gH, and gL and trap these viral proteins in the trans-Golgi network (TGN) rather than degrading them. Overall, we conclude that MARCH1/2 inhibit PRV by trapping the viral cell-to-cell fusion complex in TGN.
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