Proteomic analysis of cells in the early stages of herpes simplex virus type-1 infection reveals widespread changes in the host cell proteome

PROTEOMICS ◽  
2009 ◽  
Vol 9 (15) ◽  
pp. 3913-3927 ◽  
Author(s):  
Robin Antrobus ◽  
Kyle Grant ◽  
Bevin Gangadharan ◽  
David Chittenden ◽  
Roger D. Everett ◽  
...  
2017 ◽  
Vol 157 ◽  
pp. 17-18 ◽  
Author(s):  
Takuya Fukuoka ◽  
Yoshihiko Nakazato ◽  
Akifumi Miyake ◽  
Naotoshi Tamura ◽  
Nobuo Araki ◽  
...  

Molecules ◽  
2019 ◽  
Vol 24 (23) ◽  
pp. 4215 ◽  
Author(s):  
Wan ◽  
Wang ◽  
Chen ◽  
Zhu ◽  
Shang ◽  
...  

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.


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