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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