数字农科院2.0

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

作者： Rui Huang;Cui Hong Rao;Yuan Zhe Bai;Changqing Yu;Meng Chen;Jin Mei Peng;Shi Jia Xu;Yue Sun;Meng Fandan;Chuang Lyu;Mirwaise Khan;Tong Qing An;Zhi Jun Tian;Xue Hui Cai;Gang Wang;Yan Dong Tang

作者机构：

关键词： Cell-to-cell fusion;Furin;Glycoprotein B;Herpesvirus;MARCH1;MARCH2;Pseudorabies virus

期刊名称： Veterinary Microbiology

ISSN： 0378-1135

年卷期： 2024 年 295 卷

页码：

收录情况： SCIE（2024版）

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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