IFITM3 inhibits severe fever with thrombocytopenia syndrome virus entry and interacts with viral Gc protein
文献类型： 外文期刊
作者： Du, Shouwen 1 ; Wang, Yuhang 3 ; Wang, Jiamin 4 ; Ma, Yidan 4 ; Xu, Wang 4 ; Shi, Xiaoshuang 4 ; Li, Letian 4 ; Hao, Pengfei 4 ; Liu, Quan 1 ; Liao, Ming 1 ; Zhou, Boping 2 ; Jin, Ningyi 4 ; Wong, Yin K. 5 ; Hu, Lifen 6 ; Wang, Jigang 2 ; Liu, Wei 7 ; Li, Chang 4 ;
作者机构： 1.Guangdong Acad Agr Sci, Key Lab Livestock Dis Prevent Guangdong Prov, Guangzhou, Peoples R China
2.Jinan Univ, Shenzhen Peoples Hosp, Clin Med Coll 2, Shenzhen, Peoples R China
3.Shenzhen Bay Lab, Pingshan Translat Med Ctr, Shenzhen, Peoples R China
4.Chinese Acad Agr Sci, Changchun Vet Res Inst, Chinese Acad Med Sci, Res Unit,Key Technol Prevent & Control Virus Zoon, Changchun 130122, Peoples R China
5.Natl Univ Singapore, Yong Loo Lin Sch Med, Dept Physiol, Singapore, Singapore
6.Anhui Med Univ, Dept Infect Dis, Affiliated Hosp 1, Hefei, Peoples R China
7.Beijing Inst Microbiol & Epidemiol, State Key Lab Pathogen & Biosecur, Beijing 100071, Peoples R China
关键词： antiviral activity; Gc subunit; interferon-induced transmembrane protein 3; SFTSV; virus-IFITM3 interaction
期刊名称：JOURNAL OF MEDICAL VIROLOGY （ 影响因子：6.8； 五年影响因子：6.6 ）
ISSN： 0146-6615
年卷期： 2024 年 96 卷 3 期
页码：
收录情况： SCI
摘要： Severe fever with thrombocytopenia syndrome (SFTS) is an emerging tick-borne hemorrhagic fever disease with high fatality rate of 10%-20%. Vaccines or specific therapeutic measures remain lacking. Human interferon inducible transmembrane protein 3 (hIFITM3) is a broad-spectrum antiviral factor targeting viral entry. However, the antiviral activity of hIFITM3 against SFTS virus (SFTSV) and the functional mechanism of IFITM3 remains unclear. Here we demonstrate that endogenous IFITM3 provides protection against SFTSV infection and participates in the anti-SFTSV effect of type I and III interferons (IFNs). IFITM3 overexpression exhibits anti-SFTSV function by blocking Gn/Gc-mediated viral entry and fusion. Further studies showed that IFITM3 binds SFTSV Gc directly and its intramembrane domain (IMD) is responsible for this interaction and restriction of SFTSV entry. Mutation of two neighboring cysteines on IMD weakens IFITM3-Gc interaction and attenuates the antiviral activity of IFITM3, suggesting that IFITM3-Gc interaction may partly mediate the inhibition of SFTSV entry. Overall, our data demonstrate for the first time that hIFITM3 plays a critical role in the IFNs-mediated anti-SFTSV response, and uncover a novel mechanism of IFITM3 restriction of SFTSV infection, highlighting the potential of clinical intervention on SFTS disease.
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