Molecules | |
A Subcellular Quantitative Proteomic Analysis of Herpes Simplex Virus Type 1-Infected HEK 293T Cells | |
Liangjie Wang1  Weijuan Shang2  Weiwei Wan2  Shenglin Zhu2  Lei-Ke Zhang2  Gengfu Xiao2  Xi Chen3  | |
[1] Hubei Key Laboratory of Purification and Application of Plant Anti-Cancer Active Ingredients, School of Chemistry and Life Sciences, Hubei University of Education, Wuhan 430205, China;State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China;Wuhan Institute of Biotechnology, Wuhan 430074, China; | |
关键词: quantitative proteomics; herpes simplex virus type 1; virus–host interaction; ifitm3; chchd2; trim27; | |
DOI : 10.3390/molecules24234215 | |
来源: DOAJ |
【 摘 要 】
Herpes simplex virus type 1 (HSV-1) is widespread double-stranded DNA (dsDNA) virus that establishes life-long latency and causes diverse severe symptoms. The mechanisms of HSV-1 infection and HSV-1’s interactions with various host cells have been studied and reviewed extensively. Type I interferons were secreted by host cells upon HSV infection and play a vital role in controlling virus proliferation. A few studies, however, have focused on HSV-1 infection without the presence of interferon (IFN) signaling. In this study, HEK 293T cells with low toll-like receptor (TLR) and stimulator of interferon genes protein (STING) expression were infected with HSV-1 and subjected to a quantitative proteomic analysis. By using a subcellular fractionation strategy and high-performance mass spectrometry, a total of 6607 host proteins were quantified, of which 498 proteins were differentially regulated. A bioinformatics analysis indicated that multiple signaling pathways might be involved in HSV-1 infection. A further functional study indicated the role of Interferon-induced transmembrane protein 3 (IFITM3), Coiled-coil-helix-coiled-coil-helix domain-containing protein 2 (CHCHD2), and Tripartite motif-containing protein 27 (TRIM27) in inhibiting viral DNA replication and proliferation. Our data provide a global view of host responses to HSV-1 infection in HEK 293T cells and identify the proteins involved in the HSV-1 infection process.
【 授权许可】
Unknown