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Home / Equine Research Bank / J Virol / Equine Myxovirus Resistance Protein 2 Restricts Lentiviral R...
Journal of virology2018; 92(18); e00499-18; doi: 10.1128/JVI.00499-18

Equine Myxovirus Resistance Protein 2 Restricts Lentiviral Replication by Blocking Nuclear Uptake of Capsid Protein.

Abstract: Human myxovirus resistance protein 2 (huMxB) has been shown to be a determinant type I interferon (IFN)-induced host factor involved in the inhibition of human immunodeficiency virus type 1 (HIV-1) as well as many other primate lentiviruses. This blocking occurs after the reverse transcription of viral RNA and ahead of integration into the host DNA, which is closely connected to the ability of the protein to bind the viral capsid. To date, Mx2s derived from nonprimate animals have shown no capacity for HIV-1 suppression. In this study, we examined the restrictive effect of equine Mx2 (eqMx2) on both equine infectious anemia virus (EIAV) and HIV-1 and investigated possible mechanisms for its specific function. We demonstrated that IFN-α/β upregulates the expression of eqMx2 in equine monocyte-derived macrophages (eMDMs). The overexpression of eqMx2 significantly suppresses the replication of EIAV, HIV-1, and simian immunodeficiency viruses (SIVs) but not that of murine leukemia virus (MLV). The knockdown of eqMx2 transcription weakens the inhibition of EIAV replication by type I interferon. Interestingly, data from immunofluorescence assays suggest that the subcellular localization of eqMx2 changes following virus infection, from being dispersed in the cytoplasm to being accumulated at the nuclear envelope. Furthermore, eqMx2 blocks the nuclear uptake of the proviral genome by binding to the viral capsid. The N-terminally truncated mutant of eqMx2 lost the ability to bind the viral capsid as well as the restriction effect for lentiviruses. These results improve our understanding of the Mx2 protein in nonprimate animals. Previous research has shown that the antiviral ability of Mx2s is confined to primates, particularly humans. EIAV has been shown to be insensitive to restriction by human MxB. Here, we describe the function of equine Mx2. This protein plays an important role in the suppression of EIAV, HIV-1, and SIVs. The antiviral activity of eqMx2 depends on its subcellular location as well as its capsid binding capacity. Our results showed that following viral infection, eqMx2 changes its original cytoplasmic location and accumulates at the nuclear envelope, where it binds to the viral capsid and blocks the nuclear entry of reverse-transcribed proviral DNAs. In contrast, huMxB does not bind to the EIAV capsid and shows no EIAV restriction effect. These studies expand our understanding of the function of the equine Mx2 protein.
Copyright © 2018 Ji et al.
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Publication Date: 2018-08-29 PubMed ID: 29743377PubMed Central: PMC6146692DOI: 10.1128/JVI.00499-18Google 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 identifies the role of the equine myxovirus resistance protein 2 (eqMx2) in restricting the replication of lentiviruses such as HIV-1 by preventing the transportation of the viral genome into the host’s cell nucleus.

Research Overview

This scientific experiment conducted in-depth analyses of the antiviral capacity of the equine Mx2 protein belonging to the myxovirus resistance proteins family. The researchers particularly concentrated on eqMx2’s effect on lentiviruses replication processes, including HIV-1 and equine infectious anemia virus (EIAV).

Important Findings

  • Exposure to type I interferon (IFN-α/β) amplifies the expression of eqMx2 in equine monocyte-derived macrophages (eMDMs).
  • The overproduction of eqMx2 considerably inhibits the multiplication of EIAV, HIV-1, and simian immunodeficiency viruses (SIVs), while it does not affect murine leukemia virus (MLV) replication.
  • The reduction of eqMx2 transcription damages the action of type I interferon to inhibit EIAV replication.

Key Mechanisms

The study observed that following a viral infection, eqMx2 changes its location from being dispersed in the cell’s cytoplasm to accumulating at the nuclear envelope where it binds to the viral capsid. This process blocks the entry of the viral genome, which hampers the virus’s ability to infiltrate and replicate within the host’s cells.

Implication of the Study

The understanding of eqMx2’s role provides valuable insights into the antiviral activity of Mx2 proteins in nonprimate animals, a feature previously regarded to be present only in primates. These findings could facilitate future studies around the potential therapeutic use of Mx2 proteins in viral restrictions.

The antiviral activity of eqMx2, dependent on its subcellular location and its capacity to bind the virus’s capsid, could significantly contribute to the development of effective lentivirus suppression strategies. As eqMx2 has shown effectiveness against HIV-1, which makes this study a stepping stone for further HIV suppression experiments and treatments.

In contrast to human myxovirus resistance protein 2 (huMxB), eqMx2 has shown an ability to bind to the EIAV capsid and restrict its effect, revealing a significant difference in the functioning of primate and non-primate Mx2 proteins.

Cite This Article

APA
Ji S, Na L, Ren H, Wang Y, Wang X. (2018). Equine Myxovirus Resistance Protein 2 Restricts Lentiviral Replication by Blocking Nuclear Uptake of Capsid Protein. J Virol, 92(18), e00499-18. https://doi.org/10.1128/JVI.00499-18

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 92
Issue: 18
PII: e00499-18

Researcher Affiliations

Ji, Shuang
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Na, Lei
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Ren, Huiling
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Wang, Yujie
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Wang, Xiaojun
  • State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China wangxiaojun@caas.cn.

MeSH Terms

  • Animals
  • Capsid Proteins / antagonists & inhibitors
  • Capsid Proteins / metabolism
  • Cytoplasm / physiology
  • Cytoplasm / ultrastructure
  • Cytoplasm / virology
  • HIV-1 / genetics
  • HIV-1 / physiology
  • Horses
  • Infectious Anemia Virus, Equine / genetics
  • Infectious Anemia Virus, Equine / physiology
  • Interferon-alpha / genetics
  • Leukemia Virus, Murine / physiology
  • Macrophages / virology
  • Myxovirus Resistance Proteins / deficiency
  • Myxovirus Resistance Proteins / genetics
  • Myxovirus Resistance Proteins / metabolism
  • Nuclear Envelope / metabolism
  • Nuclear Envelope / ultrastructure
  • Simian Immunodeficiency Virus / physiology
  • Virus Replication / genetics

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Citations

This article has been cited 9 times.
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