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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

References

This article includes 51 references
  1. Haller O, Staeheli P, Schwemmle M, Kochs G. Mx GTPases: dynamin-like antiviral machines of innate immunity.. Trends Microbiol 2015 Mar;23(3):154-63.
    doi: 10.1016/j.tim.2014.12.003pubmed: 25572883google scholar: lookup
  2. Verhelst J, Hulpiau P, Saelens X. Mx proteins: antiviral gatekeepers that restrain the uninvited.. Microbiol Mol Biol Rev 2013 Dec;77(4):551-66.
    doi: 10.1128/MMBR.00024-13pmc: PMC3973384pubmed: 24296571google scholar: lookup
  3. Haller O. Dynamins are forever: MxB inhibits HIV-1.. Cell Host Microbe 2013 Oct 16;14(4):371-3.
    doi: 10.1016/j.chom.2013.10.002pubmed: 24139395google scholar: lookup
  4. Pavlovic J, Haller O, Staeheli P. Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle.. J Virol 1992 Apr;66(4):2564-9.
    pmc: PMC289059pubmed: 1548781doi: 10.1128/JVI.66.4.2564-2569.1992google scholar: lookup
  5. Xiao H, Killip MJ, Staeheli P, Randall RE, Jackson D. The human interferon-induced MxA protein inhibits early stages of influenza A virus infection by retaining the incoming viral genome in the cytoplasm.. J Virol 2013 Dec;87(23):13053-8.
    doi: 10.1128/JVI.02220-13pmc: PMC3838145pubmed: 24049170google scholar: lookup
  6. Schneider-Schaulies S, Schneider-Schaulies J, Schuster A, Bayer M, Pavlovic J, ter Meulen V. Cell type-specific MxA-mediated inhibition of measles virus transcription in human brain cells.. J Virol 1994 Nov;68(11):6910-7.
    pmc: PMC237126pubmed: 7933071doi: 10.1128/JVI.68.11.6910-6917.1994google scholar: lookup
  7. Frese M, Kochs G, Feldmann H, Hertkorn C, Haller O. Inhibition of bunyaviruses, phleboviruses, and hantaviruses by human MxA protein.. J Virol 1996 Feb;70(2):915-23.
    pmc: PMC189895pubmed: 8551631doi: 10.1128/JVI.70.2.915-923.1996google scholar: lookup
  8. Kochs G, Janzen C, Hohenberg H, Haller O. Antivirally active MxA protein sequesters La Crosse virus nucleocapsid protein into perinuclear complexes.. Proc Natl Acad Sci U S A 2002 Mar 5;99(5):3153-8.
    doi: 10.1073/pnas.052430399pmc: PMC122488pubmed: 11880649google scholar: lookup
  9. Melén K, Julkunen I. Nuclear cotransport mechanism of cytoplasmic human MxB protein.. J Biol Chem 1997 Dec 19;272(51):32353-9.
    doi: 10.1074/jbc.272.51.32353pubmed: 9405443google scholar: lookup
  10. King MC, Raposo G, Lemmon MA. Inhibition of nuclear import and cell-cycle progression by mutated forms of the dynamin-like GTPase MxB.. Proc Natl Acad Sci U S A 2004 Jun 15;101(24):8957-62.
    doi: 10.1073/pnas.0403167101pmc: PMC428454pubmed: 15184662google scholar: lookup
  11. Goujon C, Moncorgé O, Bauby H, Doyle T, Ward CC, Schaller T, Hué S, Barclay WS, Schulz R, Malim MH. Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection.. Nature 2013 Oct 24;502(7472):559-62.
    doi: 10.1038/nature12542pmc: PMC3808269pubmed: 24048477google scholar: lookup
  12. Kane M, Yadav SS, Bitzegeio J, Kutluay SB, Zang T, Wilson SJ, Schoggins JW, Rice CM, Yamashita M, Hatziioannou T, Bieniasz PD. MX2 is an interferon-induced inhibitor of HIV-1 infection.. Nature 2013 Oct 24;502(7472):563-6.
    doi: 10.1038/nature12653pmc: PMC3912734pubmed: 24121441google scholar: lookup
  13. Liu Z, Pan Q, Ding S, Qian J, Xu F, Zhou J, Cen S, Guo F, Liang C. The interferon-inducible MxB protein inhibits HIV-1 infection.. Cell Host Microbe 2013 Oct 16;14(4):398-410.
    doi: 10.1016/j.chom.2013.08.015pubmed: 24055605google scholar: lookup
  14. Fribourgh JL, Nguyen HC, Matreyek KA, Alvarez FJD, Summers BJ, Dewdney TG, Aiken C, Zhang P, Engelman A, Xiong Y. Structural insight into HIV-1 restriction by MxB.. Cell Host Microbe 2014 Nov 12;16(5):627-638.
    doi: 10.1016/j.chom.2014.09.021pmc: PMC4252739pubmed: 25312384google scholar: lookup
  15. Xu B, Kong J, Wang X, Wei W, Xie W, Yu XF. Structural insight into the assembly of human anti-HIV dynamin-like protein MxB/Mx2.. Biochem Biophys Res Commun 2015 Jan 2;456(1):197-201.
    doi: 10.1016/j.bbrc.2014.11.058pubmed: 25446123google scholar: lookup
  16. Fricke T, White TE, Schulte B, de Souza Aranha Vieira DA, Dharan A, Campbell EM, Brandariz-Nuñez A, Diaz-Griffero F. MxB binds to the HIV-1 core and prevents the uncoating process of HIV-1.. Retrovirology 2014 Aug 14;11:68.
    doi: 10.1186/s12977-014-0068-xpmc: PMC4145229pubmed: 25123063google scholar: lookup
  17. Kong J, Xu B, Wei W, Wang X, Xie W, Yu XF. Characterization of the amino-terminal domain of Mx2/MxB-dependent interaction with the HIV-1 capsid.. Protein Cell 2014 Dec;5(12):954-7.
    doi: 10.1007/s13238-014-0113-5pmc: PMC4259888pubmed: 25363729google scholar: lookup
  18. Buffone C, Schulte B, Opp S, Diaz-Griffero F. Contribution of MxB oligomerization to HIV-1 capsid binding and restriction.. J Virol 2015 Mar;89(6):3285-94.
    doi: 10.1128/JVI.03730-14pmc: PMC4337540pubmed: 25568212google scholar: lookup
  19. Dicks MD, Goujon C, Pollpeter D, Betancor G, Apolonia L, Bergeron JR, Malim MH. Oligomerization Requirements for MX2-Mediated Suppression of HIV-1 Infection.. J Virol 2016 Jan 1;90(1):22-32.
    doi: 10.1128/JVI.02247-15pmc: PMC4702540pubmed: 26446602google scholar: lookup
  20. Goujon C, Greenbury RA, Papaioannou S, Doyle T, Malim MH. A triple-arginine motif in the amino-terminal domain and oligomerization are required for HIV-1 inhibition by human MX2.. J Virol 2015 Apr;89(8):4676-80.
    doi: 10.1128/JVI.00169-15pmc: PMC4442396pubmed: 25673704google scholar: lookup
  21. Melén K, Keskinen P, Ronni T, Sareneva T, Lounatmaa K, Julkunen I. Human MxB protein, an interferon-alpha-inducible GTPase, contains a nuclear targeting signal and is localized in the heterochromatin region beneath the nuclear envelope.. J Biol Chem 1996 Sep 20;271(38):23478-86.
    doi: 10.1074/jbc.271.38.23478pubmed: 8798556google scholar: lookup
  22. Busnadiego I, Kane M, Rihn SJ, Preugschas HF, Hughes J, Blanco-Melo D, Strouvelle VP, Zang TM, Willett BJ, Boutell C, Bieniasz PD, Wilson SJ. Host and viral determinants of Mx2 antiretroviral activity.. J Virol 2014 Jul;88(14):7738-52.
    doi: 10.1128/JVI.00214-14pmc: PMC4097781pubmed: 24760893google scholar: lookup
  23. Goujon C, Moncorgé O, Bauby H, Doyle T, Barclay WS, Malim MH. Transfer of the amino-terminal nuclear envelope targeting domain of human MX2 converts MX1 into an HIV-1 resistance factor.. J Virol 2014 Aug;88(16):9017-26.
    doi: 10.1128/JVI.01269-14pmc: PMC4136259pubmed: 24899177google scholar: lookup
  24. Schulte B, Buffone C, Opp S, Di Nunzio F, De Souza Aranha Vieira DA, Brandariz-Nuñez A, Diaz-Griffero F. Restriction of HIV-1 Requires the N-Terminal Region of MxB as a Capsid-Binding Motif but Not as a Nuclear Localization Signal.. J Virol 2015 Aug;89(16):8599-610.
    doi: 10.1128/JVI.00753-15pmc: PMC4524248pubmed: 26063425google scholar: lookup
  25. Leroux C, Cadoré JL, Montelaro RC. Equine Infectious Anemia Virus (EIAV): what has HIV's country cousin got to tell us?. Vet Res 2004 Jul-Aug;35(4):485-512.
    doi: 10.1051/vetres:2004020pubmed: 15236678google scholar: lookup
  26. Yin X, Hu Z, Gu Q, Wu X, Zheng YH, Wei P, Wang X. Equine tetherin blocks retrovirus release and its activity is antagonized by equine infectious anemia virus envelope protein.. J Virol 2014 Jan;88(2):1259-70.
    doi: 10.1128/JVI.03148-13pmc: PMC3911658pubmed: 24227834google scholar: lookup
  27. 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. 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 2014 Nov;88(21):12296-310.
    doi: 10.1128/JVI.01379-14pmc: PMC4248950pubmed: 25122784google scholar: lookup
  28. Rahm N, Yap M, Snoeck J, Zoete V, Muñoz M, Radespiel U, Zimmermann E, Michielin O, Stoye JP, Ciuffi A, Telenti A. Unique spectrum of activity of prosimian TRIM5alpha against exogenous and endogenous retroviruses.. J Virol 2011 May;85(9):4173-83.
    doi: 10.1128/JVI.00075-11pmc: PMC3126249pubmed: 21345948google scholar: lookup
  29. Richardson MW, Carroll RG, Stremlau M, Korokhov N, Humeau LM, Silvestri G, Sodroski J, Riley JL. Mode of transmission affects the sensitivity of human immunodeficiency virus type 1 to restriction by rhesus TRIM5alpha.. J Virol 2008 Nov;82(22):11117-28.
    doi: 10.1128/JVI.01046-08pmc: PMC2573261pubmed: 18768965google scholar: lookup
  30. Na L, Tang YD, Liu JD, Yu CQ, Sun LK, Lin YZ, Wang XF, Wang X, Zhou JH. TRIMe7-CypA, an alternative splicing isoform of TRIMCyp in rhesus macaque, negatively modulates TRIM5α activity.. Biochem Biophys Res Commun 2014 Apr 4;446(2):470-4.
    doi: 10.1016/j.bbrc.2014.02.132pubmed: 24613845google scholar: lookup
  31. Matreyek KA, Wang W, Serrao E, Singh PK, Levin HL, Engelman A. Host and viral determinants for MxB restriction of HIV-1 infection.. Retrovirology 2014 Oct 25;11:90.
    doi: 10.1186/s12977-014-0090-zpmc: PMC4213484pubmed: 25348155google scholar: lookup
  32. Opp S, Vieira DA, Schulte B, Chanda SK, Diaz-Griffero F. MxB Is Not Responsible for the Blocking of HIV-1 Infection Observed in Alpha Interferon-Treated Cells.. J Virol 2015 Dec 30;90(6):3056-64.
    doi: 10.1128/JVI.03146-15pmc: PMC4810631pubmed: 26719253google scholar: lookup
  33. Malim MH, Bieniasz PD. HIV Restriction Factors and Mechanisms of Evasion.. Cold Spring Harb Perspect Med 2012 May;2(5):a006940.
    doi: 10.1101/cshperspect.a006940pmc: PMC3331687pubmed: 22553496google scholar: lookup
  34. Jia X, Zhao Q, Xiong Y. HIV suppression by host restriction factors and viral immune evasion.. Curr Opin Struct Biol 2015 Apr;31:106-14.
    doi: 10.1016/j.sbi.2015.04.004pmc: PMC4476947pubmed: 25939065google scholar: lookup
  35. Sheehy AM, Gaddis NC, Choi JD, Malim MH. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.. Nature 2002 Aug 8;418(6898):646-50.
    doi: 10.1038/nature00939pubmed: 12167863google scholar: lookup
  36. Stremlau M, Owens CM, Perron MJ, Kiessling M, Autissier P, Sodroski J. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys.. Nature 2004 Feb 26;427(6977):848-53.
    doi: 10.1038/nature02343pubmed: 14985764google scholar: lookup
  37. Neil SJ, Zang T, Bieniasz PD. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu.. Nature 2008 Jan 24;451(7177):425-30.
    doi: 10.1038/nature06553pubmed: 18200009google scholar: lookup
  38. Hrecka K, Hao C, Gierszewska M, Swanson SK, Kesik-Brodacka M, Srivastava S, Florens L, Washburn MP, Skowronski J. Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein.. Nature 2011 Jun 29;474(7353):658-61.
    doi: 10.1038/nature10195pmc: PMC3179858pubmed: 21720370google scholar: lookup
  39. Wang X, Han Y, Dang Y, Fu W, Zhou T, Ptak RG, Zheng YH. Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus replication.. J Biol Chem 2010 May 7;285(19):14346-55.
    doi: 10.1074/jbc.M110.109314pmc: PMC2863248pubmed: 20215113google scholar: lookup
  40. Rosa A, Chande A, Ziglio S, De Sanctis V, Bertorelli R, Goh SL, McCauley SM, Nowosielska A, Antonarakis SE, Luban J, Santoni FA, Pizzato M. HIV-1 Nef promotes infection by excluding SERINC5 from virion incorporation.. Nature 2015 Oct 8;526(7572):212-7.
    doi: 10.1038/nature15399pmc: PMC4861059pubmed: 26416734google scholar: lookup
  41. Usami Y, Wu Y, Göttlinger HG. SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef.. Nature 2015 Oct 8;526(7572):218-23.
    doi: 10.1038/nature15400pmc: PMC4600458pubmed: 26416733google scholar: lookup
  42. Yamashita M, Emerman M. Retroviral infection of non-dividing cells: old and new perspectives.. Virology 2006 Jan 5;344(1):88-93.
    doi: 10.1016/j.virol.2005.09.012pubmed: 16364740google scholar: lookup
  43. Yamashita M, Perez O, Hope TJ, Emerman M. Evidence for direct involvement of the capsid protein in HIV infection of nondividing cells.. PLoS Pathog 2007 Oct 26;3(10):1502-10.
    doi: 10.1371/journal.ppat.0030156pmc: PMC2042020pubmed: 17967060google scholar: lookup
  44. Yamashita M, Emerman M. Capsid is a dominant determinant of retrovirus infectivity in nondividing cells.. J Virol 2004 Jun;78(11):5670-8.
    doi: 10.1128/JVI.78.11.5670-5678.2004pmc: PMC415837pubmed: 15140964google scholar: lookup
  45. Campbell EM, Hope TJ. HIV-1 capsid: the multifaceted key player in HIV-1 infection.. Nat Rev Microbiol 2015 Aug;13(8):471-83.
    doi: 10.1038/nrmicro3503pmc: PMC4876022pubmed: 26179359google scholar: lookup
  46. Lin YZ, Cao XZ, Li L, Li L, Jiang CG, Wang XF, Ma J, Zhou JH. The pathogenic and vaccine strains of equine infectious anemia virus differentially induce cytokine and chemokine expression and apoptosis in macrophages.. Virus Res 2011 Sep;160(1-2):274-82.
    doi: 10.1016/j.virusres.2011.06.028pubmed: 21782860google scholar: lookup
  47. Zhang Z, Ma J, Zhang X, Su C, Yao QC, Wang X. Equine Infectious Anemia Virus Gag Assembly and Export Are Directed by Matrix Protein through trans-Golgi Networks and Cellular Vesicles.. J Virol 2016 Feb 15;90(4):1824-38.
    doi: 10.1128/JVI.02814-15pmc: PMC4734017pubmed: 26637458google scholar: lookup
  48. Yamamoto N, Tanaka C, Wu Y, Chang MO, Inagaki Y, Saito Y, Naito T, Ogasawara H, Sekigawa I, Hayashida Y. Analysis of human immunodeficiency virus type 1 integration by using a specific, sensitive and quantitative assay based on real-time polymerase chain reaction.. Virus Genes 2006 Feb;32(1):105-13.
    doi: 10.1007/s11262-005-5851-2pubmed: 16525741google scholar: lookup
  49. Hu Z, Chang H, Chu X, Li S, Wang M, Wang X. Identification and characterization of a common B-cell epitope on EIAV capsid proteins.. Appl Microbiol Biotechnol 2016 Dec;100(24):10531-10542.
    doi: 10.1007/s00253-016-7817-9pubmed: 27660181google scholar: lookup
  50. Liu GJ, Wang JP, Xiao JC, Zhao ZW, Zheng YT. Preparation and characterization of three monoclonal antibodies against HIV-1 p24 capsid protein.. Cell Mol Immunol 2007 Jun;4(3):203-8.
    pubmed: 17601374
  51. Bolte S, Cordelières FP. A guided tour into subcellular colocalization analysis in light microscopy.. J Microsc 2006 Dec;224(Pt 3):213-32.
    doi: 10.1111/j.1365-2818.2006.01706.xpubmed: 17210054google scholar: lookup

Citations

This article has been cited 10 times.
  1. Wang XF, Zhang X, Ma W, Li J, Wang X. Host cell restriction factors of equine infectious anemia virus. Virol Sin 2023 Aug;38(4):485-496.
    doi: 10.1016/j.virs.2023.07.001pubmed: 37419416google scholar: lookup
  2. Betancor G. You Shall Not Pass: MX2 Proteins Are Versatile Viral Inhibitors. Vaccines (Basel) 2023 May 3;11(5).
    doi: 10.3390/vaccines11050930pubmed: 37243034google scholar: lookup
  3. Duan Y, Wang X, Sun K, Lin Y, Wang X, Chen K, Yang G, Wang X, Du C. SYNJ2BP Improves the Production of Lentiviral Envelope Protein by Facilitating the Formation of Mitochondrion-Associated Endoplasmic Reticulum Membrane. J Virol 2022 Oct 26;96(20):e0054922.
    doi: 10.1128/jvi.00549-22pubmed: 36197105google scholar: lookup
  4. Wang Y, Ma G, Wang XF, Na L, Guo X, Zhang J, Liu C, Du C, Qi T, Lin Y, Wang X. Keap1 recognizes EIAV early accessory protein Rev to promote antiviral defense. PLoS Pathog 2022 Feb;18(2):e1009986.
    doi: 10.1371/journal.ppat.1009986pubmed: 35139135google scholar: lookup
  5. Saito A, Yamashita M. HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules. Retrovirology 2021 Oct 26;18(1):32.
    doi: 10.1186/s12977-021-00577-xpubmed: 34702294google scholar: lookup
  6. Boso G, Kozak CA. Retroviral Restriction Factors and Their Viral Targets: Restriction Strategies and Evolutionary Adaptations. Microorganisms 2020 Dec 11;8(12).
    doi: 10.3390/microorganisms8121965pubmed: 33322320google scholar: lookup
  7. Bai B, Wang XF, Zhang M, Na L, Zhang X, Zhang H, Yang Z, Wang X. The N-glycosylation of Equine Tetherin Affects Antiviral Activity by Regulating Its Subcellular Localization. Viruses 2020 Feb 16;12(2).
    doi: 10.3390/v12020220pubmed: 32079099google scholar: lookup
  8. Li L, Xue M, Fu F, Yin L, Feng L, Liu P. IFN-Lambda 3 Mediates Antiviral Protection Against Porcine Epidemic Diarrhea Virus by Inducing a Distinct Antiviral Transcript Profile in Porcine Intestinal Epithelia. Front Immunol 2019;10:2394.
    doi: 10.3389/fimmu.2019.02394pubmed: 31681286google scholar: lookup
  9. Wang Y, Zhang H, Na L, Du C, Zhang Z, Zheng YH, Wang X. ANP32A and ANP32B are key factors in the Rev-dependent CRM1 pathway for nuclear export of HIV-1 unspliced mRNA. J Biol Chem 2019 Oct 18;294(42):15346-15357.
    doi: 10.1074/jbc.RA119.008450pubmed: 31444273google scholar: lookup
  10. Schimmich C, Vabret A, Zientara S, Valle-Casuso JC. Equine Infectious Anemia Virus Cellular Partners Along the Viral Cycle. Viruses 2024 Dec 24;17(1).
    doi: 10.3390/v17010005pubmed: 39861793google scholar: lookup
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