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Journal of virology2014; 88(21); 12296-12310; doi: 10.1128/JVI.01379-14

Equine viperin restricts equine infectious anemia virus replication by inhibiting the production and/or release of viral Gag, Env, and receptor via distortion of the endoplasmic reticulum.

Abstract: Viperin is an endoplasmic reticulum (ER)-associated multifunctional protein that regulates virus replication and possesses broad antiviral activity. In many cases, viperin interferes with the trafficking and budding of viral structural proteins by distorting the membrane transportation system. The lentivirus equine infectious anemia virus (EIAV) has been studied extensively. In this study, we examined the restrictive effect of equine viperin (eViperin) on EIAV replication and investigated the possible molecular basis of this restriction to obtain insights into the effect of this cellular factor on retroviruses. We demonstrated that EIAV infection of primary equine monocyte-derived macrophages (eMDMs) upregulated the expression of eViperin. The overexpression of eViperin significantly inhibited the replication of EIAV in eMDMs, and knockdown of eViperin transcription enhanced the replication of EIAV in eMDMs by approximately 45.8%. Further experiments indicated that eViperin restricts EIAV at multiple steps of viral replication. The overexpression of eViperin inhibited EIAV Gag release. Both the α-helix domain and radical S-adenosylmethionine (SAM) domain were required for this activity. However, the essential motifs in SAM were different from those reported for the inhibition of HIV-1 Gag by human viperin. Furthermore, eViperin disrupted the synthesis of both EIAV Env and receptor, which consequently inhibited viral production and entry, respectively, and this disruption was dependent on the eViperin α-helix domain. Using immunofluorescence assays and electron microscopy, we demonstrated that the α-helix domain is responsible for the distortion of the endoplasmic reticulum (ER). Finally, EIAV did not exhibit counteracting eViperin at the protein level. Objective: In previous studies, viperin was indicated as restricting virus replications primarily by the inhibition of virus budding. Here, we show that viperin may have multiple antiviral mechanisms, including the reduction of EIAV Gag budding and Env expression, and these activities are dependent on different viperin domains. We especially demonstrate that the overexpression of viperin inhibits EIAV entry by decreasing the level of virus receptor. Therefore, viperin restriction of viruses is determined largely by the dependence of virus on the cellular membrane transportation system.
Copyright © 2014, American Society for Microbiology. All Rights Reserved.
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Publication Date: 2014-08-13 PubMed ID: 25122784PubMed Central: PMC4248950DOI: 10.1128/JVI.01379-14Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research demonstrates that the overexpression of a protein known as equine viperin (eViperin) significantly reduces the replication of the Equine Infectious Anemia Virus (EIAV) in primary equine monocyte-derived macrophages. It works by distorting the ER transportation system and preventing the release of viral Gag, Env, and receptor, all essential to the EIAV’s reproductive processes.

Understanding Equine Viperin and EIAV

  • The study focuses on the proteins involved in the replication of Equine Infectious Anemia Virus (EIAV), a lentivirus that affects horses.
  • Viperin, an endoplasmic reticulum (ER)-associated multifunctional protein, regulates virus replication and demonstrates broad antiviral activity. In this study, the focus is specifically on equine viperin (eViperin).
  • EIAV infection in horses’ primary monocyte-derived macrophages (eMDMs) boosts the production of eViperin.

Equine Viperin’s Inhibitive Effect on EIAV

  • Overexpression of eViperin significantly hampers the replication of EIAV in eMDMs.
  • The suppression of eViperin transcription augments the replication of EIAV in eMDMs by approximately 45.8%.
  • eViperin obstructs EIAV at multiple stages of viral replication.
  • eViperin obstructs the release of the viral Gag, a critical process in the replication of the virus. Both the α-helix domain and radical S-adenosylmethionine (SAM) domain of the protein are necessary for this function.

Viperin Effects on Cellular Systems and EIAV Counteraction

  • eViperin disrupts both EIAV Env and receptor synthesis, which inhibit viral reproduction and entry into the host cell, respectively. The α-helix domain of the protein is indispensable for such disruption.
  • Immunofluorescence assays and electron microscopic techniques indicated that the α-helix domain is responsible for distorted endoplasmic reticulum (ER).
  • EIAV does not exhibit counteraction to eViperin at the protein level, indicating its efficacy in curbing the spread of the virus.
  • The study concluded that eViperin’s restriction activities are contingent on the virus’s dependency on the host’s cellular membrane transportation system. This might open novel avenues for antiviral therapeutic development.

Cite This Article

APA
Tang YD, Na L, Zhu CH, Shen N, Yang F, Fu XQ, Wang YH, Fu LH, Wang JY, Lin YZ, Wang XF, Wang X, Zhou JH, Li CY. (2014). Equine viperin restricts equine infectious anemia virus replication by inhibiting the production and/or release of viral Gag, Env, and receptor via distortion of the endoplasmic reticulum. J Virol, 88(21), 12296-12310. https://doi.org/10.1128/JVI.01379-14

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 88
Issue: 21
Pages: 12296-12310

Researcher Affiliations

Tang, Yan-Dong
  • Biotechnology Institute of Southern Medical University, Guangzhou, China State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Na, Lei
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Zhu, Chun-Hui
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Shen, Nan
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Yang, Fei
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Fu, Xian-Qiu
  • The First Affiliated Hospital of Harbin Medical University, Harbin, China.
Wang, Yu-Hong
  • The First Affiliated Hospital of Harbin Medical University, Harbin, China.
Fu, Li-Hua
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Wang, Jia-Yi
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Lin, Yue-Zhi
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Wang, Xue-Feng
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Wang, Xiaojun
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China.
Zhou, Jian-Hua
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of Chinese Academy of Agricultural Sciences, Harbin, China Harbin Pharmaceutical Group Biovaccine Company, Harbin, China jianhua_uc@126.com chengyaoli@hotmail.com.
Li, Cheng-Yao
  • Biotechnology Institute of Southern Medical University, Guangzhou, China jianhua_uc@126.com chengyaoli@hotmail.com.

MeSH Terms

  • Animals
  • Cells, Cultured
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum / ultrastructure
  • Endoplasmic Reticulum / virology
  • Fluorescent Antibody Technique
  • HIV-1
  • Horses
  • Host-Pathogen Interactions
  • Infectious Anemia Virus, Equine / immunology
  • Infectious Anemia Virus, Equine / physiology
  • Macrophages / immunology
  • Macrophages / virology
  • Microscopy, Electron
  • Viral Proteins / metabolism
  • Virus Release
  • Virus Replication

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