Human MARCH1, 2, and 8 block Ebola virus envelope glycoprotein cleavage via targeting furin P domain

文献类型： 外文期刊

第一作者： Yu, Changqing

作者： Yu, Changqing;Li, Xuemei;Bai, Yuanzhe;Tang, Yan-Dong;Tan, Wenbo;Bai, Yu;Zhou, Yulong;Zhai, Jingbo;Xue, Mengzhou;Zheng, Chunfu;Zheng, Chunfu;Liu, Qiang;Tang, Yan-Dong;Zheng, Chunfu;Liu, Qiang

作者机构：

关键词： cleavage; Ebola virus; envelope glycoprotein; furin; MARCH

期刊名称：JOURNAL OF MEDICAL VIROLOGY （ 影响因子：12.7； 五年影响因子：8.5 ）

ISSN： 0146-6615

年卷期： 2024 年 96 卷 2 期

页码：

收录情况： SCI

摘要： Membrane-associated RING-CH (MARCH) family proteins were recently reported to inhibit viral replication through multiple modes. Previous work showed that human MARCH8 blocked Ebola virus (EBOV) glycoprotein (GP) maturation. Our study here demonstrates that human MARCH1 and MARCH2 share a similar pattern to MARCH8 in restricting EBOV GP-pseudotyped viral infection. Human MARCH1 and MARCH2 retain EBOV GP at the trans-Golgi network, reduce its cell surface display, and impair EBOV GP-pseudotyped virions infectivity. Furthermore, we uncover that the host proprotein convertase furin could interact with human MARCH1/2 and EBOV GP intracellularly. Importantly, the furin P domain is verified to be recognized by MARCH1/2/8, which is critical for their blocking activities. Besides, bovine MARCH2 and murine MARCH1 also impair EBOV GP proteolytic processing. Altogether, our findings confirm that MARCH1/2 proteins of different mammalian origins showed a relatively conserved feature in blocking EBOV GP cleavage, which could provide clues for subsequent MARCHs antiviral studies and may facilitate the development of novel strategies to antagonize enveloped virus infection.

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