2. Academic Validation
  3. The Interaction Mechanism Between Herpes Simplex Virus 1 Glycoprotein D and Host Antiviral Protein Viperin

The Interaction Mechanism Between Herpes Simplex Virus 1 Glycoprotein D and Host Antiviral Protein Viperin

  • Front Immunol. 2019 Dec 11;10:2810. doi: 10.3389/fimmu.2019.02810.
Meili Li 1 2,  Zongmin Liao 1 2 3,  Zuo Xu 1 2,  Xingmei Zou 1 2,  Yuanfang Wang 1 2,  Hao Peng 1 2,  Yiwen Li 1 2,  Xiaowen Ou 1 2,  Yangxi Deng 1 2,  Yingjie Guo 1 2,  Weidong Gan 1 2,  Tao Peng 4 5,  Daixiong Chen 1 2,  Mingsheng Cai 1 2
Affiliations

Affiliations

  • 1 Guangdong Provincial Key Laboratory of Allergy and Clinical Immunology, Second Affiliated Hospital of Guangzhou Medical University, Guangzhou, China.
  • 2 Department of Pathogenic Biology and Immunology, School of Basic Medical Science, Sino-French Hoffmann Institute, Guangzhou Medical University, Guangzhou, China.
  • 3 Department of Scientific Research and Education, Yuebei People's Hospital, Shaoguan, China.
  • 4 State Key Laboratory of Respiratory Diseases, School of Basic Medical Science, Sino-French Hoffmann Institute, Guangzhou Medical University, Guangzhou, China.
  • 5 South China Vaccine Corporation Limited, Guangzhou, China.
PMID: 31921110 DOI: 10.3389/fimmu.2019.02810
Abstract

Viperin is an interferon-inducible protein that responsible for a variety of Antiviral responses to different viruses. Our previous study has shown that the ribonuclease UL41 of herpes simplex virus 1 (HSV-1) can degrade the mRNA of viperin to promote HSV-1 replication. However, it is not clear whether other HSV-1 encoded proteins can regulate the function of viperin. Here, one novel viperin associated protein, glycoprotein D (gD), was identified. To verify the interaction between gD and viperin, gD and viperin expression plasmids were firstly co-transfected into COS-7 cells, and fluorescence microscope showed they co-localized at the perinuclear region, then this potential interaction was confirmed by co-immunoprecipitation (Co-IP) assays. Moreover, confocal microscopy demonstrated that gD and viperin co-localized at the Golgi body and lipid droplets. Furthermore, dual-luciferase reporter and Co-IP assays showed gD and viperin interaction leaded to the increase of IRF7-mediated IFN-β expression through promoting viperin and IRAK1 interaction and facilitating K63-linked IRAK1 polyubiquitination. Nevertheless, gD inhibited TRAF6-induced NF-κB activity by decreasing the interaction of viperin and TRAF6. In addition, gD restrained viperin-mediated interaction between IRAK1 and TRAF6. Eventually, gD and viperin interaction was corroborated to significantly inhibit the proliferation of HSV-1. Taken together, this study would open up new avenues toward delineating the function and physiological significance of gD and viperin during HSV-1 replication cycle.

Keywords

IFN-β; NF-κB; gD; herpes simplex virus 1; viperin.

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