A Subcellular Quantitative Proteomic Analysis of Herpes Simplex Virus Type 1-Infected HEK 293T Cells
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 interf...
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Published in | Molecules (Basel, Switzerland) Vol. 24; no. 23; p. 4215 |
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Abstract | 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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AbstractList | 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. |
Author | Chen, Xi Zhang, Lei-Ke Zhu, Shenglin Wang, Liangjie Shang, Weijuan Wan, Weiwei Xiao, Gengfu |
AuthorAffiliation | 3 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; wangliangjie@hue.edu.cn 4 Department of Biological Mass Spectrometry, Wuhan Institute of Biotechnology, Wuhan 430074, China; chenxi@spec-ally.com 2 University of the Chinese Academy of Sciences, Beijing 100049, China 5 Medical Research Institute, Wuhan University, Wuhan 430074, China 1 State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China; weiwei.wan.cas.whiov@gmail.com (W.W.); cqubiozsl@gmail.com (S.Z.); shangweijuan@wh.iov.cn (W.S.) |
AuthorAffiliation_xml | – name: 4 Department of Biological Mass Spectrometry, Wuhan Institute of Biotechnology, Wuhan 430074, China; chenxi@spec-ally.com – name: 5 Medical Research Institute, Wuhan University, Wuhan 430074, China – name: 2 University of the Chinese Academy of Sciences, Beijing 100049, China – name: 3 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; wangliangjie@hue.edu.cn – name: 1 State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China; weiwei.wan.cas.whiov@gmail.com (W.W.); cqubiozsl@gmail.com (S.Z.); shangweijuan@wh.iov.cn (W.S.) |
Author_xml | – sequence: 1 givenname: Weiwei surname: Wan fullname: Wan, Weiwei organization: University of the Chinese Academy of Sciences, Beijing 100049, China – sequence: 2 givenname: Liangjie surname: Wang fullname: Wang, Liangjie organization: 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 – sequence: 3 givenname: Xi surname: Chen fullname: Chen, Xi organization: Medical Research Institute, Wuhan University, Wuhan 430074, China – sequence: 4 givenname: Shenglin surname: Zhu fullname: Zhu, Shenglin organization: University of the Chinese Academy of Sciences, Beijing 100049, China – sequence: 5 givenname: Weijuan surname: Shang fullname: Shang, Weijuan organization: State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China – sequence: 6 givenname: Gengfu surname: Xiao fullname: Xiao, Gengfu organization: University of the Chinese Academy of Sciences, Beijing 100049, China – sequence: 7 givenname: Lei-Ke surname: Zhang fullname: Zhang, Lei-Ke organization: University of the Chinese Academy of Sciences, Beijing 100049, China |
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Keywords | IFITM3 herpes simplex virus type 1 CHCHD2 virus–host interaction Quantitative proteomics TRIM27 |
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SubjectTerms | Bioinformatics chchd2 Cytoplasm Deoxyribonucleic acid DNA DNA biosynthesis DNA Replication - physiology DNA viruses DNA, Viral - biosynthesis DNA, Viral - genetics DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Fractionation Gene expression Glycoproteins HEK293 Cells Herpes simplex herpes simplex virus type 1 Herpes viruses Herpesvirus 1, Human - physiology Humans ifitm3 Infections Interferon Kinases Latency Mass spectrometry Mass spectroscopy Membrane Proteins - genetics Membrane Proteins - metabolism Nuclear Proteins - genetics Nuclear Proteins - metabolism Peptides Proteins Proteomics quantitative proteomics Regulation RNA polymerase RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Signal transduction Stimulators Toll-like receptors Transcription Factors - genetics Transcription Factors - metabolism trim27 Viral infections Virus Replication - physiology Viruses virus–host interaction |
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Title | A Subcellular Quantitative Proteomic Analysis of Herpes Simplex Virus Type 1-Infected HEK 293T Cells |
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