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Molecules. 2019 Nov 20;24(23). pii: E4215. doi: 10.3390/molecules24234215.

A Subcellular Quantitative Proteomic Analysis of Herpes Simplex Virus Type 1-Infected HEK 293T Cells.

Wan W1,2, Wang L3, Chen X4,5, Zhu S1,2, Shang W1, Xiao G1,2, Zhang LK1,2.

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State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
University of the Chinese Academy of Sciences, Beijing 100049, China.
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.
Wuhan Institute of Biotechnology, Wuhan 430074, China.
Medical Research Institute, Wuhan University, Wuhan 430074, China.


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.


CHCHD2; IFITM3; Quantitative proteomics; TRIM27; herpes simplex virus type 1; virus–host interaction

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Conflict of interest statement

The authors declare no conflicts of interest. The founding sponsors had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript; and in the decision to publish the results.

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