FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Viruses / Equine Infectious Anemia Virus Cellular Partners Along the V...
Viruses2024; 17(1); 5; doi: 10.3390/v17010005

Equine Infectious Anemia Virus Cellular Partners Along the Viral Cycle.

Abstract: Equine infectious anemia virus (EIAV) is the simplest described within the family, related to the human immunodeficiency viruses (HIV-1 and HIV-2). There is an important interplay between host cells and viruses. Viruses need to hijack cellular proteins for their viral cycle completion and some cellular proteins are antiviral agents interfering with viral replication. HIV cellular partners have been extensively studied and described, with a special attention to host proteins able to inhibit specific steps of the viral cycle, called restriction factors. Viruses develop countermeasures against these restriction factors. Here, we aim to describe host cellular protein partners of EIAV viral replication, being proviral or antiviral. A comprehensive vision of the interactions between the virus and specific host's proteins can help with the discovery of new targets for the design of therapeutics. Studies performed on HIV-1 can provide insights into the functioning of EIAV, as well as differences, as both types of virus research can benefit from each other.
Get Full Text
Publication Date: 2024-12-24 PubMed ID: 39861793PubMed Central: PMC11769393DOI: 10.3390/v17010005Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article
  • Review

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 article investigates the relationship between host cells and the equine infectious anemia virus (EIAV), which is similar to the human immunodeficiency viruses (HIV-1 and HIV-2). The study emphasises the importance of the interactions between viruses and their host’s cellular proteins, which could guide the development of new therapeutic strategies.

Interaction Between Viruses and Host Cells

  • The article starts by examining the interactions between viruses and host cells. Viruses rely on the proteins within a host cell to complete their replication cycle. This interaction between the virus and host cell often has significant implications for the development and severity of the disease.

HIV and EIAV: Comparative Studies

  • As the EIAV is related to the HIV-1 and HIV-2 viruses, the authors draw many comparisons between the two. They note that studies on HIV’s cellular partners are extensive, offering vast amounts of information on host proteins that inhibit specific steps of the viral replication cycle, known as restriction factors.
  • In this context, the authors propose that insights from HIV-1 studies could be beneficial for understanding the workings of EIAV, despite their differences. The interplay between the two fields of research promises to be mutually beneficial.

Importance of Cellular Protein Partners

  • The authors intend to identify and detail host cellular protein partners involved in EIAV viral replication. The role these partners play might be either in favor of the virus (proviral) or against it (antiviral).
  • Understanding the intricate interactions between the virus and these host proteins could guide the design of new therapeutic strategies. The ability to harness or inhibit these proteins could potentially help healthcare professionals manage or even prevent the virus.

Conclusion

  • In this study, the authors seek to provide an in-depth understanding of the interactions taking place during the EIAV’s replication cycle. Given the relationship between EIAV and the better-studied HIV, they believe the findings from HIV research can enrich our understanding and intervention strategies for EIAV, and vice versa.

Cite This Article

APA
(2024). Equine Infectious Anemia Virus Cellular Partners Along the Viral Cycle. Viruses, 17(1), 5. https://doi.org/10.3390/v17010005

Publication

Viruses
ISSN: 1999-4915
NlmUniqueID: 101509722
Country: Switzerland
Language: English
Volume: 17
Issue: 1
PII: 5

Researcher Affiliations

MeSH Terms

  • Infectious Anemia Virus, Equine / physiology
  • Virus Replication
  • Animals
  • Humans
  • Horses
  • Equine Infectious Anemia / virology
  • Host-Pathogen Interactions
  • HIV-1 / physiology

Grant Funding

  • 21 E01168 I 00061963 / Ru00e9gion Normandie

Conflict of Interest Statement

The authors declare no conflicts of interest.

References

This article includes 93 references
  1. Issel CJ, Foil LD. Studies on Equine Infectious Anemia Virus Transmission by Insects. J. Am. Vet. Med. Assoc. 1984;184:293–297.
    pubmed: 6321420
  2. Harrold SM, Cook SJ, Cook RF, Rushlow KE, Issel CJ, Montelaro RC. Tissue Sites of Persistent Infection and Active Replication of Equine Infectious Anemia Virus during Acute Disease and Asymptomatic Infection in Experimentally Infected Equids. J. Virol. 2000;74:3112–3121.
    doi: 10.1128/JVI.74.7.3112-3121.2000pmc: PMC111810pubmed: 10708426google scholar: lookup
  3. Hammond SA, Li F, McKeon BM, Cook SJ, Issel CJ, Montelaro RC. Immune Responses and Viral Replication in Long-Term Inapparent Carrier Ponies Inoculated with Equine Infectious Anemia Virus. J. Virol. 2000;74:5968–5981.
    doi: 10.1128/JVI.74.13.5968-5981.2000pmc: PMC112093pubmed: 10846078google scholar: lookup
  4. Kono Y, Hirasawa K, Fukunaga Y, Taniguchi T. Recrudescence of Equine Infectious Anemia by Treatment with Immunosuppressive Drugs. Natl. Inst. Anim. Health. Q. 1976;16:8–15.
    pubmed: 177894
  5. Tumas DB, Hines MT, Perryman LE, Davis WC, McGuire TC. Corticosteroid Immunosuppression and Monoclonal Antibody-Mediated CD5+ T Lymphocyte Depletion in Normal and Equine Infectious Anaemia Virus-Carrier Horses. J. General. Virol. 1994;75:959–968.
    doi: 10.1099/0022-1317-75-5-959pubmed: 7513746google scholar: lookup
  6. Wang XF, Zhang X, Ma W, Li J, Wang X. Host Cell Restriction Factors of Equine Infectious Anemia Virus. Virol. Sin. 2023;38:485–496.
    doi: 10.1016/j.virs.2023.07.001pmc: PMC10436108pubmed: 37419416google scholar: lookup
  7. Leroux C, Cadoré JL, Montelaro RC. Equine Infectious Anemia Virus (EIAV): What Has HIV’s Country Cousin Got to Tell Us?. Vet. Res. 2004;35:485–512.
    doi: 10.1051/vetres:2004020pubmed: 15236678google scholar: lookup
  8. Li F, Puffer BA, Montelaro RC. The S2 Gene of Equine Infectious Anemia Virus Is Dispensable for Viral Replication in Vitro. J. Virol. 1998;72:8344–8348.
    doi: 10.1128/JVI.72.10.8344-8348.1998pmc: PMC110207pubmed: 9733881google scholar: lookup
  9. Li F, Leroux C, Craigo JK, Cook SJ, Issel CJ, Montelaro RC. The S2 Gene of Equine Infectious Anemia Virus Is a Highly Conserved Determinant of Viral Replication and Virulence Properties in Experimentally Infected Ponies. J. Virol. 2000;74:573–579.
    doi: 10.1128/JVI.74.1.573-579.2000pmc: PMC111574pubmed: 10590152google scholar: lookup
  10. Fagerness AJ, Flaherty MT, Perry ST, Jia B, Payne SL, Fuller FJ. The S2 Accessory Gene of Equine Infectious Anemia Virus Is Essential for Expression of Disease in Ponies. Virology 2006;349:22–30.
    doi: 10.1016/j.virol.2005.12.041pubmed: 16503341google scholar: lookup
  11. Li G, De Clercq E. HIV Genome-Wide Protein Associations: A Review of 30 Years of Research. Microbiol. Mol. Biol. Rev. 2016;80:679–731.
    doi: 10.1128/MMBR.00065-15pmc: PMC4981665pubmed: 27357278google scholar: lookup
  12. Beisel CE, Edwards JF, Dunn LL, Rice NR. Analysis of Multiple mRNAs from Pathogenic Equine Infectious Anemia Virus (EIAV) in an Acutely Infected Horse Reveals a Novel Protein, Ttm, Derived from the Carboxy Terminus of the EIAV Transmembrane Protein. J. Virol. 1993;67:832–842.
    doi: 10.1128/jvi.67.2.832-842.1993pmc: PMC237437pubmed: 8419648google scholar: lookup
  13. Li J, Zhang X, Bai B, Zhang M, Ma W, Lin Y, Wang X, Wang XF. Identification of a Novel Post-Transcriptional Transactivator from the Equine Infectious Anemia Virus. J. Virol. 2022;96:e01210-22.
    doi: 10.1128/jvi.01210-22pmc: PMC9769392pubmed: 36448796google scholar: lookup
  14. Zhang X, Li J, Zhang M, Bai B, Ma W, Lin Y, Guo X, Wang XF, Wang X. A Novel, Fully Spliced, Accessory Gene in Equine Lentivirus with Distinct Rev-Responsive Element. J. Virol. 2022;96:e00986-22.
    doi: 10.1128/jvi.00986-22pmc: PMC9517694pubmed: 36069548google scholar: lookup
  15. Zhang B, Jin S, Jin J, Li F, Montelaro RC. A Tumor Necrosis Factor Receptor Family Protein Serves as a Cellular Receptor for the Macrophage-Tropic Equine Lentivirus. Proc. Natl. Acad. Sci. USA 2005;102:9918–9923.
    doi: 10.1073/pnas.0501560102pmc: PMC1174982pubmed: 15985554google scholar: lookup
  16. Dharan A, Bachmann N, Talley S, Zwikelmaier V, Campbell EM. Nuclear Pore Blockade Reveals That HIV-1 Completes Reverse Transcription and Uncoating in the Nucleus. Nat. Microbiol. 2020;5:1088–1095.
    doi: 10.1038/s41564-020-0735-8pmc: PMC9286700pubmed: 32483230google scholar: lookup
  17. Arhel NJ. Early HIV Replication Revisited. Nat. Microbiol. 2020;5:1065–1066.
    doi: 10.1038/s41564-020-0784-zpubmed: 32839574google scholar: lookup
  18. Vodicka MA. Determinants for Lentiviral Infection of Non-Dividing Cells. Somat. Cell Mol. Genet. 2001;26:35–49.
    doi: 10.1023/A:1021022629126pubmed: 12465461google scholar: lookup
  19. Suzuki Y, Craigie R. The Road to Chromatin—Nuclear Entry of Retroviruses. Nat. Rev. Microbiol. 2007;5:187–196.
    doi: 10.1038/nrmicro1579pubmed: 17304248google scholar: lookup
  20. Demeulemeester J, De Rijck J, Gijsbers R, Debyser Z. Retroviral Integration: Site Matters: Mechanisms and Consequences of Retroviral Integration Site Selection. Bioessays 2015;37:1202–1214.
    doi: 10.1002/bies.201500051pmc: PMC5053271pubmed: 26293289google scholar: lookup
  21. Dakshinamoorthy A, Asmita A, Senapati S. Comprehending the Structure, Dynamics, and Mechanism of Action of Drug-Resistant HIV Protease. ACS Omega 2023;8:9748–9763.
    doi: 10.1021/acsomega.2c08279pmc: PMC10034783pubmed: 36969469google scholar: lookup
  22. Pettit SC, Michael SF, Swanstrom R. The Specificity of the HIV-1 Protease. Perspect. Drug Discov. Des. 1993;1:69–83.
    doi: 10.1007/BF02171656google scholar: lookup
  23. Colomer-Lluch M, Ruiz A, Moris A, Prado JG. Restriction Factors: From Intrinsic Viral Restriction to Shaping Cellular Immunity Against HIV-1. Front. Immunol. 2018;9:2876.
    doi: 10.3389/fimmu.2018.02876pmc: PMC6291751pubmed: 30574147google scholar: lookup
  24. Oaks JL, McGuire TC, Ulibarri C, Crawford TB. Equine Infectious Anemia Virus Is Found in Tissue Macrophages during Subclinical Infection. J. Virol. 1998;72:7263–7269.
    doi: 10.1128/JVI.72.9.7263-7269.1998pmc: PMC109949pubmed: 9696821google scholar: lookup
  25. Sellon DC, Walker KM, Russell KE, Perry ST, Covington P, Fuller FJ. Equine Infectious Anemia Virus Replication Is Upregulated during Differentiation of Blood Monocytes from Acutely Infected Horses. J. Virol. 1996;70:590–594.
    doi: 10.1128/jvi.70.1.590-594.1996pmc: PMC189850pubmed: 8523576google scholar: lookup
  26. Maury W. Monocyte Maturation Controls Expression of Equine Infectious Anemia Virus. J. Virol. 1994;68:6270–6279.
    doi: 10.1128/jvi.68.10.6270-6279.1994pmc: PMC237047pubmed: 8083967google scholar: lookup
  27. Jin S, Zhang B, Weisz OA, Montelaro RC. Receptor-Mediated Entry by Equine Infectious Anemia Virus Utilizes a pH-Dependent Endocytic Pathway. J. Virol. 2005;79:14489–14497.
    doi: 10.1128/JVI.79.23.14489-14497.2005pmc: PMC1287590pubmed: 16282448google scholar: lookup
  28. Brindley MA, Maury W. Endocytosis and a Low-pH Step Are Required for Productive Entry of Equine Infectious Anemia Virus. J. Virol. 2005;79:14482–14488.
    doi: 10.1128/JVI.79.23.14482-14488.2005pmc: PMC1287591pubmed: 16282447google scholar: lookup
  29. Brindley MA, Maury W. Equine Infectious Anemia Virus Entry Occurs through Clathrin-Mediated Endocytosis. J. Virol. 2008;82:1628–1637.
    doi: 10.1128/JVI.01754-07pmc: PMC2258727pubmed: 18057237google scholar: lookup
  30. Shimojima M, Miyazawa T, Ikeda Y, McMonagle EL, Haining H, Akashi H, Takeuchi Y, Hosie MJ, Willett BJ. Use of CD134 as a Primary Receptor by the Feline Immunodeficiency Virus. Science 2004;303:1192–1195.
    doi: 10.1126/science.1092124pubmed: 14976315google scholar: lookup
  31. De Parseval A, Chatterji U, Sun P, Elder JH. Feline Immunodeficiency Virus Targets Activated CD4 T Cells by Using CD134 as a Binding Receptor. Proc. Natl. Acad. Sci. USA 2004;101:13044–13049.
    doi: 10.1073/pnas.0404006101pmc: PMC516514pubmed: 15326292google scholar: lookup
  32. Zhang B, Sun C, Jin S, Cascio M, Montelaro RC. Mapping of Equine Lentivirus Receptor 1 Residues Critical for Equine Infectious Anemia Virus Envelope Binding. J. Virol. 2008;82:1204–1213.
    doi: 10.1128/JVI.01393-07pmc: PMC2224449pubmed: 18032504google scholar: lookup
  33. Best S, Tissier PL, Towers G, Stoye JP. Positional Cloning of the Mouse Retrovirus Restriction Gene Fvl. Nature 1996;382:826–829.
    doi: 10.1038/382826a0pubmed: 8752279google scholar: lookup
  34. Hatziioannou T. Restriction of Multiple Divergent Retroviruses by Lv1 and Ref1. EMBO J. 2003;22:385–394.
    doi: 10.1093/emboj/cdg042pmc: PMC140727pubmed: 12554640google scholar: lookup
  35. Hatziioannou T, Perez-Caballero D, Yang A, Cowan S, Bieniasz PD. Retrovirus Resistance Factors Ref1 and Lv1 Are Species-Specific Variants of TRIM5α. Proc. Natl. Acad. Sci. USA 2004;101:10774–10779.
    doi: 10.1073/pnas.0402361101pmc: PMC490010pubmed: 15249685google scholar: lookup
  36. Yap MW, Colbeck E, Ellis SA, Stoye JP. Evolution of the Retroviral Restriction Gene Fv1: Inhibition of Non-MLV Retroviruses. PLoS Pathog. 2014;10:e1003968.
    doi: 10.1371/journal.ppat.1003968pmc: PMC3948346pubmed: 24603659google scholar: lookup
  37. Ganser-Pornillos BK, Pornillos O. Restriction of HIV-1 and Other Retroviruses by TRIM5. Nat. Rev. Microbiol. 2019;17:546–556.
    doi: 10.1038/s41579-019-0225-2pmc: PMC6858284pubmed: 31312031google scholar: lookup
  38. Zhang F, Hatziioannou T, Perez-Caballero D, Derse D, Bieniasz PD. Antiretroviral Potential of Human Tripartite Motif-5 and Related Proteins. Virology 2006;353:396–409.
    doi: 10.1016/j.virol.2006.05.035pubmed: 16828831google scholar: lookup
  39. Sebastian S, Grütter C, De Castillia CS, Pertel T, Olivari S, Grütter MG, Luban J. An Invariant Surface Patch on the TRIM5α PRYSPRY Domain Is Required for Retroviral Restriction but Dispensable for Capsid Binding. J. Virol. 2009;83:3365–3373.
    doi: 10.1128/JVI.00432-08pmc: PMC2655600pubmed: 19153241google scholar: lookup
  40. Diaz-Griffero F, Kar A, Lee M, Stremlau M, Poeschla E, Sodroski J. Comparative Requirements for the Restriction of Retrovirus Infection by TRIM5α and TRIMCyp. Virology 2007;369:400–410.
    doi: 10.1016/j.virol.2007.08.032pmc: PMC2153441pubmed: 17920096google scholar: lookup
  41. Meier K, Jaguva Vasudevan AA, Zhang Z, Bähr A, Kochs G, Häussinger D, Münk C. Equine MX2 Is a Restriction Factor of Equine Infectious Anemia Virus (EIAV). Virology 2018;523:52–63.
    doi: 10.1016/j.virol.2018.07.024pubmed: 30081309google scholar: lookup
  42. Ji S, Na L, Ren H, Wang Y, Wang X. Equine Myxovirus Resistance Protein 2 Restricts Lentiviral Replication by Blocking Nuclear Uptake of Capsid Protein. J. Virol. 2018;92:e00499-18.
    doi: 10.1128/JVI.00499-18pmc: PMC6146692pubmed: 29743377google scholar: lookup
  43. White TE, Brandariz-Nuñez A, Valle-Casuso JC, Amie S, Nguyen L, Kim B, Brojatsch J, Diaz-Griffero F. Contribution of SAM and HD Domains to Retroviral Restriction Mediated by Human SAMHD1. Virology 2013;436:81–90.
    doi: 10.1016/j.virol.2012.10.029pmc: PMC3767443pubmed: 23158101google scholar: lookup
  44. Mereby SA, Maehigashi T, Holler JM, Kim DH, Schinazi RF, Kim B. Interplay of Ancestral Non-Primate Lentiviruses with the Virus-Restricting SAMHD1 Proteins of Their Hosts. J. Biol. Chem. 2018;293:16402–16412.
    doi: 10.1074/jbc.RA118.004567pmc: PMC6200947pubmed: 30181218google scholar: lookup
  45. Ren H, Yin X, Su C, Guo M, Wang XF, Na L, Lin Y, Wang X. Equine Lentivirus Counteracts SAMHD1 Restriction by Rev-Mediated Degradation of SAMHD1 via the BECN1-Dependent Lysosomal Pathway. Autophagy 2021;17:2800–2817.
    doi: 10.1080/15548627.2020.1846301pmc: PMC8525956pubmed: 33172327google scholar: lookup
  46. 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;418:646–650.
    doi: 10.1038/nature00939pubmed: 12167863google scholar: lookup
  47. Kao S, Khan MA, Miyagi E, Plishka R, Buckler-White A, Strebel K. The Human Immunodeficiency Virus Type 1 Vif Protein Reduces Intracellular Expression and Inhibits Packaging of APOBEC3G (CEM15), a Cellular Inhibitor of Virus Infectivity. J. Virol. 2003;77:11398–11407.
    doi: 10.1128/JVI.77.21.11398-11407.2003pmc: PMC229358pubmed: 14557625google scholar: lookup
  48. Münk C, Beck T, Zielonka J, Hotz-Wagenblatt A, Chareza S, Battenberg M, Thielebein J, Cichutek K, Bravo IG, O’Brien SJ. Functions, Structure, and Read-through Alternative Splicing of Feline APOBEC3 Genes. Genome Biol. 2008;9:R48.
    doi: 10.1186/gb-2008-9-3-r48pmc: PMC2397500pubmed: 18315870google scholar: lookup
  49. Zielonka J, Marino D, Hofmann H, Yuhki N, Löchelt M, Münk C. Vif of Feline Immunodeficiency Virus from Domestic Cats Protects against APOBEC3 Restriction Factors from Many Felids. J. Virol. 2010;84:7312–7324.
    doi: 10.1128/JVI.00209-10pmc: PMC2898260pubmed: 20444897google scholar: lookup
  50. LaRue RS, Lengyel J, Jónsson SR, Andrésdóttir V, Harris RS. Lentiviral Vif Degrades the APOBEC3Z3/APOBEC3H Protein of Its Mammalian Host and Is Capable of Cross-Species Activity. J. Virol. 2010;84:8193–8201.
    doi: 10.1128/JVI.00685-10pmc: PMC2916508pubmed: 20519393google scholar: lookup
  51. Bogerd HP, Tallmadge RL, Oaks JL, Carpenter S, Cullen BR. Equine Infectious Anemia Virus Resists the Antiretroviral Activity of Equine APOBEC3 Proteins through a Packaging-Independent Mechanism. J. Virol. 2008;82:11889–11901.
    doi: 10.1128/JVI.01537-08pmc: PMC2583693pubmed: 18818324google scholar: lookup
  52. Zielonka J, Bravo IG, Marino D, Conrad E, Perković M, Battenberg M, Cichutek K, Münk C. Restriction of Equine Infectious Anemia Virus by Equine APOBEC3 Cytidine Deaminases. J. Virol. 2009;83:7547–7559.
    doi: 10.1128/JVI.00015-09pmc: PMC2708611pubmed: 19458006google scholar: lookup
  53. Matreyek KA, Yücel SS, Li X, Engelman A. Nucleoporin NUP153 Phenylalanine-Glycine Motifs Engage a Common Binding Pocket within the HIV-1 Capsid Protein to Mediate Lentiviral Infectivity. PLoS Pathog. 2013;9:e1003693.
    doi: 10.1371/journal.ppat.1003693pmc: PMC3795039pubmed: 24130490google scholar: lookup
  54. Krishnan L, Matreyek KA, Oztop I, Lee K, Tipper CH, Li X, Dar MJ, KewalRamani VN, Engelman A. The Requirement for Cellular Transportin 3 (TNPO3 or TRN-SR2) during Infection Maps to Human Immunodeficiency Virus Type 1 Capsid and Not Integrase. J. Virol. 2010;84:397–406.
    doi: 10.1128/JVI.01899-09pmc: PMC2798409pubmed: 19846519google scholar: lookup
  55. Logue EC, Taylor KT, Goff PH, Landau NR. The Cargo-Binding Domain of Transportin 3 Is Required for Lentivirus Nuclear Import. J. Virol. 2011;85:12950–12961.
    doi: 10.1128/JVI.05384-11pmc: PMC3233122pubmed: 21976643google scholar: lookup
  56. Valle-Casuso JC, Di Nunzio F, Yang Y, Reszka N, Lienlaf M, Arhel N, Perez P, Brass AL, Diaz-Griffero F. TNPO3 Is Required for HIV-1 Replication after Nuclear Import but Prior to Integration and Binds the HIV-1 Core. J. Virol. 2012;86:5931–5936.
    doi: 10.1128/JVI.00451-12pmc: PMC3347269pubmed: 22398280google scholar: lookup
  57. Marshall HM, Ronen K, Berry C, Llano M, Sutherland H, Saenz D, Bickmore W, Poeschla E, Bushman FD. Role of PSIP1/LEDGF/P75 in Lentiviral Infectivity and Integration Targeting. PLoS ONE 2007;2:e1340.
    doi: 10.1371/journal.pone.0001340pmc: PMC2129110pubmed: 18092005google scholar: lookup
  58. Hacker CV, Vink CA, Wardell TW, Lee S, Treasure P, Kingsman SM, Mitrophanous KA, Miskin JE. The Integration Profile of EIAV-Based Vectors. Mol. Ther. 2006;14:536–545.
    doi: 10.1016/j.ymthe.2006.06.006pubmed: 16950499google scholar: lookup
  59. Cherepanov P. LEDGF/P75 Interacts with Divergent Lentiviral Integrases and Modulates Their Enzymatic Activity in Vitro. Nucleic Acids Res. 2007;35:113–124.
    doi: 10.1093/nar/gkl885pmc: PMC1802576pubmed: 17158150google scholar: lookup
  60. Herrmann CH, Rice AP. Lentivirus Tat Proteins Specifically Associate with a Cellular Protein Kinase, TAK, That Hyperphosphorylates the Carboxyl-Terminal Domain of the Large Subunit of RNA Polymerase II: Candidate for a Tat Cofactor. J. Virol. 1995;69:1612–1620.
    doi: 10.1128/jvi.69.3.1612-1620.1995pmc: PMC188757pubmed: 7853496google scholar: lookup
  61. Carroll R, Martarano L, Derse D. Identification of Lentivirus Tat Functional Domains through Generation of Equine Infectious Anemia Virus/Human Immunodeficiency Virus Type 1 Tat Gene Chimeras. J. Virol. 1991;65:3460–3467.
    doi: 10.1128/jvi.65.7.3460-3467.1991pmc: PMC241330pubmed: 1645777google scholar: lookup
  62. Taube R, Fujinaga K, Irwin D, Wimmer J, Geyer M, Peterlin BM. Interactions between Equine Cyclin T1, Tat, and TAR Are Disrupted by a Leucine-to-Valine Substitution Found in Human Cyclin T1. J. Virol. 2000;74:892–898.
    doi: 10.1128/JVI.74.2.892-898.2000pmc: PMC111610pubmed: 10623752google scholar: lookup
  63. Suñé C, Goldstrohm AC, Peng J, Price DH, Garcia-Blanco MA. An in Vitro Transcription System That Recapitulates Equine Infectious Anemia Virus Tat-Mediated Inhibition of Human Immunodeficiency Virus Type 1 Tat Activity Demonstrates a Role for Positive Transcription Elongation Factor b and Associated Proteins in the Mechanism of Tat Activation. Virology 2000;274:356–366.
    doi: 10.1006/viro.2000.0480pubmed: 10964778google scholar: lookup
  64. Fridell RA, Partin KM, Carpenter S, Cullen BR. Identification of the Activation Domain of Equine Infectious Anemia Virus Rev. J. Virol. 1993;67:7317–7323.
    doi: 10.1128/jvi.67.12.7317-7323.1993pmc: PMC238195pubmed: 8230455google scholar: lookup
  65. Gontarek RR, Derse D. Interactions among SR Proteins, an Exonic Splicing Enhancer, and a Lentivirus Rev Protein Regulate Alternative Splicing. Mol. Cell. Biol. 1996;16:2325–2331.
    doi: 10.1128/MCB.16.5.2325pmc: PMC231220pubmed: 8628299google scholar: lookup
  66. Belshan M, Park GS, Bilodeau P, Stoltzfus CM, Carpenter S. Binding of Equine Infectious Anemia Virus Rev to an Exon Splicing Enhancer Mediates Alternative Splicing and Nuclear Export of Viral mRNAs. Mol. Cell. Biol. 2000;20:3550–3557.
    doi: 10.1128/MCB.20.10.3550-3557.2000pmc: PMC85647pubmed: 10779344google scholar: lookup
  67. Chung H, Derse D. Binding Sites for Rev and ASF/SF2 Map to a 55-Nucleotide Purine-Rich Exonic Element in Equine Infectious Anemia Virus RNA. J. Biol. Chem. 2001;276:18960–18967.
    doi: 10.1074/jbc.M008996200pubmed: 11278454google scholar: lookup
  68. Liao HJ, Baker CC, Princler GL, Derse D. Cis-Acting and Trans-Acting Modulation of Equine Infectious Anemia Virus Alternative RNA Splicing. Virology 2004;323:131–140.
    doi: 10.1016/j.virol.2003.12.028pubmed: 15165825google scholar: lookup
  69. Venkatesh LK, Gettemeier T, Chinnadurai G. A Nuclear Kinesin-like Protein Interacts with and Stimulates the Activity of the Leucine-Rich Nuclear Export Signal of the Human Immunodeficiency Virus Type 1 Rev Protein. J. Virol. 2003;77:7236–7243.
    doi: 10.1128/JVI.77.13.7236-7243.2003pmc: PMC164832pubmed: 12805422google scholar: lookup
  70. Kiss A, Li L, Gettemeier T, Venkatesh LK. Functional Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 Rev Nuclear Export Signal with Its Cofactors. Virology 2003;314:591–600.
    doi: 10.1016/S0042-6822(03)00531-2pubmed: 14554087google scholar: lookup
  71. Tang YD, Na L, Zhu CH, Shen N, Yang F, Fu XQ, Wang YH, Fu LH, Wang JY, Lin YZ. 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;88:12296–12310.
    doi: 10.1128/JVI.01379-14pmc: PMC4248950pubmed: 25122784google scholar: lookup
  72. Gizzi AS, Grove TL, Arnold JJ, Jose J, Jangra RK, Garforth SJ, Du Q, Cahill SM, Dulyaninova NG, Love JD. A Naturally Occurring Antiviral Ribonucleotide Encoded by the Human Genome. Nature 2018;558:610–614.
    doi: 10.1038/s41586-018-0238-4pmc: PMC6026066pubmed: 29925952google scholar: lookup
  73. Li M, Kao E, Gao X, Sandig H, Limmer K, Pavon-Eternod M, Jones TE, Landry S, Pan T, Weitzman MD. Codon-Usage-Based Inhibition of HIV Protein Synthesis by Human Schlafen 11. Nature 2012;491:125–128.
    doi: 10.1038/nature11433pmc: PMC3705913pubmed: 23000900google scholar: lookup
  74. Lin YZ, Sun LK, Zhu DT, Hu Z, Wang XF, Du C, Wang YH, Wang XJ, Zhou JH. Equine Schlafen 11 Restricts the Production of Equine Infectious Anemia Virus via a Codon Usage-Dependent Mechanism. Virology 2016;495:112–121.
    doi: 10.1016/j.virol.2016.04.024pubmed: 27200480google scholar: lookup
  75. Yi B, Tanaka YL, Cornish D, Kosako H, Butlertanaka EP, Sengupta P, Lippincott-Schwartz J, Hultquist JF, Saito A, Yoshimura SH. Host ZCCHC3 Blocks HIV-1 Infection and Production through a Dual Mechanism. iScience 2024;27:109107.
    doi: 10.1016/j.isci.2024.109107pmc: PMC10879702pubmed: 38384847google scholar: lookup
  76. Hu Z, Wu X, Ge J, Wang X. Inhibition of Virus Replication and Induction of Human Tetherin Gene Expression by Equine IFN-A1. Vet. Immunol. Immunopathol. 2013;156:107–113.
    doi: 10.1016/j.vetimm.2013.09.009pubmed: 24144682google scholar: lookup
  77. 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;88:1259–1270.
    doi: 10.1128/JVI.03148-13pmc: PMC3911658pubmed: 24227834google scholar: lookup
  78. Dietrich I, McMonagle EL, Petit SJ, Vijayakrishnan S, Logan N, Chan CN, Towers GJ, Hosie MJ, Willett BJ. Feline Tetherin Efficiently Restricts Release of Feline Immunodeficiency Virus but Not Spreading of Infection. J. Virol. 2011;85:5840–5852.
    doi: 10.1128/JVI.00071-11pmc: PMC3126296pubmed: 21490095google scholar: lookup
  79. Yin X, Guo M, Gu Q, Wu X, Wei P, Wang X. Antiviral Potency and Functional Analysis of Tetherin Orthologues Encoded by Horse and Donkey. Virol. J. 2014;11:151.
    doi: 10.1186/1743-422X-11-151pmc: PMC4152588pubmed: 25158826google scholar: lookup
  80. 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;12:220.
    doi: 10.3390/v12020220pmc: PMC7077275pubmed: 32079099google scholar: lookup
  81. Puffer BA, Watkins SC, Montelaro RC. Equine Infectious Anemia Virus Gag Polyprotein Late Domain Specifically Recruits Cellular AP-2 Adapter Protein Complexes during Virion Assembly. J. Virol. 1998;72:10218–10221.
    doi: 10.1128/JVI.72.12.10218-10221.1998pmc: PMC110572pubmed: 9811764google scholar: lookup
  82. Strack B, Calistri A, Craig S, Popova E, Göttlinger HG. AIP1/ALIX Is a Binding Partner for HIV-1 P6 and EIAV P9 Functioning in Virus Budding. Cell 2003;114:689–699.
    doi: 10.1016/S0092-8674(03)00653-6pubmed: 14505569google scholar: lookup
  83. Luttge BG, Shehu-Xhilaga M, Demirov DG, Adamson CS, Soheilian F, Nagashima K, Stephen AG, Fisher RJ, Freed EO. Molecular Characterization of Feline Immunodeficiency Virus Budding. J. Virol. 2008;82:2106–2119.
    doi: 10.1128/JVI.02337-07pmc: PMC2258934pubmed: 18094166google scholar: lookup
  84. Martin-Serrano J, Yaravoy A, Perez-Caballero D, Bieniasz PD. Divergent Retroviral Late-Budding Domains Recruit Vacuolar Protein Sorting Factors by Using Alternative Adaptor Proteins. Proc. Natl. Acad. Sci. USA 2003;100:12414–12419.
    doi: 10.1073/pnas.2133846100pmc: PMC218772pubmed: 14519844google scholar: lookup
  85. Zhai Q, Fisher RD, Chung HY, Myszka DG, Sundquist WI, Hill CP. Structural and Functional Studies of ALIX Interactions with YPXnL Late Domains of HIV-1 and EIAV. Nat. Struct. Mol. Biol. 2008;15:43–49.
    doi: 10.1038/nsmb1319pubmed: 18066081google scholar: lookup
  86. Zhou X, Pan S, Sun L, Corvera J, Lin SH, Kuang J. The HIV-1 P6/EIAV P9 Docking Site in Alix Is Autoinhibited as Revealed by a Conformation-Sensitive Anti-Alix Monoclonal Antibody. Biochem. J. 2008;414:215–220.
    doi: 10.1042/BJ20080642pubmed: 18476810google scholar: lookup
  87. Zhou X, Si J, Corvera J, Gallick GE, Kuang J. Decoding the Intrinsic Mechanism That Prohibits ALIX Interaction with ESCRT and Viral Proteins. Biochem. J. 2010;432:525–538.
    doi: 10.1042/BJ20100862pmc: PMC4391464pubmed: 20929444google scholar: lookup
  88. Joshi A, Garg H, Ablan SD, Freed EO. Evidence of a Role for Soluble N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor (SNARE) Machinery in HIV-1 Assembly and Release. J. Biol. Chem. 2011;286:29861–29871.
    doi: 10.1074/jbc.M111.241521pmc: PMC3191027pubmed: 21680744google scholar: lookup
  89. Usami Y, Wu Y, Göttlinger HG. SERINC3 and SERINC5 Restrict HIV-1 Infectivity and Are Counteracted by Nef. Nature 2015;526:218–223.
    doi: 10.1038/nature15400pmc: PMC4600458pubmed: 26416733google scholar: lookup
  90. Chande A, Cuccurullo EC, Rosa A, Ziglio S, Carpenter S, Pizzato M. S2 from Equine Infectious Anemia Virus Is an Infectivity Factor Which Counteracts the Retroviral Inhibitors SERINC5 and SERINC3. Proc. Natl. Acad. Sci. USA 2016;113:13197–13202.
    doi: 10.1073/pnas.1612044113pmc: PMC5135340pubmed: 27803322google scholar: lookup
  91. Ahmad I, Li S, Li R, Chai Q, Zhang L, Wang B, Yu C, Zheng YH. The Retroviral Accessory Proteins S2, Nef, and glycoMA Use Similar Mechanisms for Antagonizing the Host Restriction Factor SERINC5. J. Biol. Chem. 2019;294:7013–7024.
    doi: 10.1074/jbc.RA119.007662pmc: PMC6497950pubmed: 30862674google scholar: lookup
  92. Wang Y, Ma G, Wang XF, Na L, Guo X, Zhang J, Liu C, Du C, Qi T, Lin Y. Keap1 Recognizes EIAV Early Accessory Protein Rev to Promote Antiviral Defense. PLoS Pathog. 2022;18:e1009986.
    doi: 10.1371/journal.ppat.1009986pmc: PMC8863222pubmed: 35139135google scholar: lookup
  93. Covaleda L, Gno BT, Fuller FJ, Payne SL. Identification of Cellular Proteins Interacting with Equine Infectious Anemia Virus S2 Protein. Virus Res. 2010;151:235–239.
    doi: 10.1016/j.virusres.2010.04.007pmc: PMC2897910pubmed: 20417672google scholar: lookup

Citations

This article has been cited 0 times.
Subscribe to our newsletter
Join 99,357 horse owners like you who receive our email updates on horse health and nutrition.