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Novel interacting proteins identified by tandem affinity purification and mass spectrometry associated with IFITM3 protein during PDCoV infection

文献类型： 外文期刊

作者： Li, Cheng 1 ; Guo, Xiao-ran 1 ; Dong, Zhi-min 1 ; Gao, Yu-jin 4 ; Li, Xiu-li 5 ; Zhang, Li 1 ; Zheng, Hong-qing 6 ; Wang, Li-li 1 ; Lu, Chao 1 ; Tian, Xiang-xue 1 ; Yan, Ming-hua 1 ;

作者机构： 1.Tianjin Acad Agr Sci, Inst Anim Sci & Vet, Tianjin Key Lab Anim Mol Breeding & Biotechnol, Tianjin 300381, Peoples R China

2.Tianjin Observat & Expt Site Natl Anim Hlth, Tianjin 300381, Peoples R China

3.Natl Data Ctr Anim Hlth, Tianjin 300381, Peoples R China

4.Gansu Agr Univ, Coll Vet Med, Lanzhou 730070, Peoples R China

5.Tianjin Acad Agr Sci, Inst Agroprod Safety & Nutr, Tianjin 300381, Peoples R China

6.Xianyang Vocat Tech Coll, Inst Anim Husb & Vet Med, Key Lab Anim Epidem Dis Diagnost Lab Mol Biol Xian, Xianyang 712000, Shaanxi, Peoples R China

关键词： Porcine deltacoronavirus; IFITM3; Innate immunity

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：7.7； 五年影响因子：7.7 ）

ISSN： 0141-8130

年卷期： 2024 年 277 卷

页码：

收录情况： SCI

摘要： Interferon-induced transmembrane 3 (IFITM3) is a membrane-associated protein that exhibits antiviral activities against a wide range of viruses through interactions with other cellular and viral proteins. However, knowledge of the mechanisms of IFITM3 in Porcine deltacoronavirus (PDCoV) infection has been lacking. In this study, we demonstrate that IFN-alpha treatment induces the upregulation of IFITM3 activity and thus attenuates PDCoV infection. PDCoV replication is inhibited in a dose-dependent manner by IFITM3 overexpression. To clarify the novel roles of IFITM3 during PDCoV infection, proteins that interact with IFITM3 were screened by TAP/MS in an ST cell line stably expressing IFITM3 via a lentivirus. We identified known and novel candidate IFITM3binding proteins and analyzed the protein complexes using GO annotation, KEGG pathway analysis, and protein interaction network analysis. A total of 362 cellular proteins associate with IFITM3 during the first 24 h postinfection. Of these proteins, the relationship between IFITM3 and Rab9a was evaluated by immunofluorescence colocalization analysis using confocal microscopy. IFITM3 partially colocalized with Rab9a and Rab9a exhibited enhanced colocalization following PDCoV infection. We also demonstrated that IFITM3 interacts specifically with Rab9a. Our results considerably expand the protein networks of IFITM3, suggesting that IFITM3 participates in multiple cellular processes during PDCoV infection.

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