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IFITM1 is a host restriction factor that inhibits porcine epidemic diarrhea virus infection

文献类型： 外文期刊

作者： Cheng, Jiahao 1 ; He, Jiayi 1 ; Feng, Simeng 1 ; Tan, Lei 1 ; Bai, Binghan 1 ; Dong, Wei 1 ; Li, Bin 4 ; Wen, Lixin 1 ; Wang, Aibing 1 ; Yuan, Xiaomin 1 ;

作者机构： 1.Hunan Agr Univ HUNAU, Coll Vet Med, Changsha 410128, Hunan, Peoples R China

2.PCB Biotechnol LLC, Rockville, MD 20852 USA

3.Yangtze Univ, Coll Anim Sci, Jingzhou 434100, Peoples R China

4.Jiangsu Acad Agr Sci, Inst Vet Med, Nanjing 210014, Jiangsu, Peoples R China

5.Inst Yunnan Circular Agr Ind, Kunming 650201, Yunnan, Peoples R China

6.Changsha Green Leaf Bio Technol Co LTD, Changsha 410119, Hunan, Peoples R China

关键词： Innate immunity; Interferon-induced transmembrane protein 1; Porcine epidemic diarrhea virus; Antiviral infection; Immune-gold labeling

期刊名称：JOURNAL OF NANOBIOTECHNOLOGY （ 影响因子：12.6； 五年影响因子：12.3 ）

ISSN：

年卷期： 2024 年 22 卷 1 期

页码：

收录情况： SCI

摘要： BackgroundPorcine epidemic diarrhea virus (PEDV) infection and transmission pose a serious threat to the global swine industry. The search for a new host factor with anti-PEDV effect may be an effective potential target for the development of novel antiviral drugs. Interferon-induced transmembrane proteins (IFITMs) play a crucial role in the innate immune response triggered by viral infection, and it has been suggested that IFITMs can block the early stages of viral replication, but the mechanism of action is currently unclear. The current study sheds light on the role of IFITM1 in PEDV infection. Specifically, overexpression of IFITM1 suppresses PEDV proliferation in IPEC-J2 cells, while knockdown of IFITM1 has the opposite effect. Collectively, these findings underscore IFITM1's inhibitory role in PEDV infection, with critical implications for the residues and structural motifs within its CTD.ResultsThe study demonstrates that IFITM1, an interferon-induced transmembrane protein, plays a critical role in the antiviral response against Porcine Epidemic Diarrhea Virus (PEDV). Notably: Overexpression of IFITM1 suppresses PEDV proliferation.IFITM1 co-localizes with PEDV virions in the cytoplasm surrounding the nucleus.Immunocolloidal gold electron microscopy reveals IFITM proteins embedded on the surface of PEDV virions.IFITM1 directly interacts with the N protein of PEDV.C-terminal domain mutations in IFITM1 compromise its inhibitory function against PEDV, with specific amino acid residues playing a pronounced role.These findings enhance our understanding of innate immunity and antiviral defense mechanisms, with potential implications for therapeutic strategies against PEDV infection.ConclusionsThe study establishes IFITM1 as a key player in the antiviral response against PEDV. Its inhibitory function, co-localization with virions, and interaction with the N protein provide valuable insights. Notably, the CTD mutations of IFITM1 have a fundamental impact on its modulatory action. These findings contribute to our understanding of innate immunity and antiviral defense mechanisms, with potential implications for therapeutic strategies against PEDV infection.

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