FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Virus Res / Identification of cellular proteins interacting with equine ...
Virus research2010; 151(2); 235-239; doi: 10.1016/j.virusres.2010.04.007

Identification of cellular proteins interacting with equine infectious anemia virus S2 protein.

Abstract: The macrophage-tropic lentivirus, equine infectious anemia virus (EIAV), encodes the small auxiliary protein S2 from a short open reading frame that overlaps the amino terminus of env EIAV S2 is dispensable for virus replication in cultured cells but is required for disease production. S2 is approximately 7 kDa and has no overall amino acid sequence homology to other cellular or viral proteins. Therefore it is likely that S2 plays a role as an adaptor protein. To further investigate S2 function we performed a yeast-2-hybrid screen to identify cellular proteins that interact with EIAV S2. The screen identified two human cellular proteins, amplified in osteosarcoma (OS-9) and proteasome 26S ATPase subunit 3 (PSMC3) that interact with S2. The equine homologues of these proteins were cloned and their interactions with S2 confirmed using co-immunoprecipitation assays. We identified two OS-9 isoforms that interact with S2 and a third splice variant that does not, indicating a region of OS-9 apparently required for the S2 interaction. The roles of these cellular proteins during EIAV infection have not been determined.
Copyright 2010 Elsevier B.V. All rights reserved.
Get Full Text
Publication Date: 2010-04-24 PubMed ID: 20417672PubMed Central: PMC2897910DOI: 10.1016/j.virusres.2010.04.007Google 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
  • Research Support
  • N.I.H.
  • Extramural

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.

This research investigates interactions between certain cellular proteins and the S2 protein of equine infectious anemia virus (EIAV), a virus primarily affecting horses, to better understand the S2 protein’s functions.

Research Context

  • The study focuses on EIAV, a lentivirus affecting horses. The virus encodes a small accessory protein named S2 that has no known sequence similarities to other viral or cellular proteins.
  • Previous research suggested that while the S2 protein isn’t necessary for the virus to replicate in labs, it’s crucial for the virus to cause disease.

Research Methodology

  • The research team utilized a tool called yeast-2-hybrid screening to identify cellular proteins that interact with EIAV’s S2 protein.
  • Through this screening, two human cellular proteins amplified in osteosarcoma (OS-9) and proteasome 26S ATPase subunit 3 (PSMC3) were identified as interacting with the S2 protein.
  • The team cloned the equine versions (homologues) of these proteins and confirmed their interactions with S2 through additional tests (co-immunoprecipitation assays).

Key Findings

  • The researchers found two forms (isoforms) of OS-9 that interact with the EIAV S2 protein.
  • A third form of OS-9 was identified that did not interact with the S2 protein, suggesting that there are specific parts of the OS-9 protein required for interaction with the S2 protein.
  • The exact roles of these cellular proteins during EIAV infection are not yet clear. This indicates further research is needed to elucidate how these interactions affect EIAV infection and disease progression.

Implications of the Study

  • Understanding the cellular counterparts of viral proteins like EIAV’s S2 protein can elucidate the mechanisms through which viruses cause diseases.
  • By identifying cellular proteins that interact with viral proteins, potential therapeutic targets may be uncovered, aiding in the development of more effective treatments.

Cite This Article

APA
Covaleda L, Gno BT, Fuller FJ, Payne SL. (2010). Identification of cellular proteins interacting with equine infectious anemia virus S2 protein. Virus Res, 151(2), 235-239. https://doi.org/10.1016/j.virusres.2010.04.007

Publication

Virus research
ISSN: 1872-7492
NlmUniqueID: 8410979
Country: Netherlands
Language: English
Volume: 151
Issue: 2
Pages: 235-239

Researcher Affiliations

Covaleda, Lina
  • Department of Pathobiology, Texas A&M University, Texas Veterinary Medical College, MS4467, College Station, TX 77843-4467, USA.
Gno, Bich-Ty
    Fuller, Fredrick J
      Payne, Susan L

        MeSH Terms

        • Animals
        • Equidae
        • Host-Pathogen Interactions
        • Humans
        • Immunoprecipitation
        • Infectious Anemia Virus, Equine / pathogenicity
        • Molecular Sequence Data
        • Protein Interaction Mapping
        • Sequence Analysis, DNA
        • Two-Hybrid System Techniques
        • Viral Proteins / metabolism
        • Virulence Factors / metabolism

        Grant Funding

        • R01 CA059278 / NCI NIH HHS
        • R01 CA059278-11 / NCI NIH HHS
        • CA-59278 / NCI NIH HHS

        References

        This article includes 29 references
        1. Alcock F, Swanton E. Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins.. J Mol Biol 2009 Jan 30;385(4):1032-42.
          pubmed: 19084021doi: 10.1016/j.jmb.2008.11.045google scholar: lookup
        2. Barak O, Aronheim A, Shaul Y. HBV X protein targets HIV Tat-binding protein 1.. Virology 2001 Apr 25;283(1):110-20.
          pubmed: 11312667doi: 10.1006/viro.2001.0883google scholar: lookup
        3. Baek JH, Mahon PC, Oh J, Kelly B, Krishnamachary B, Pearson M, Chan DA, Giaccia AJ, Semenza GL. OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha.. Mol Cell 2005 Feb 18;17(4):503-12.
          pubmed: 15721254doi: 10.1016/j.molcel.2005.01.011google scholar: lookup
        4. Bernasconi R, Pertel T, Luban J, Molinari M. A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal.. J Biol Chem 2008 Jun 13;283(24):16446-54.
          pmc: PMC3762559pubmed: 18417469doi: 10.1074/jbc.m802272200google scholar: lookup
        5. Clements JE, Payne SL. Molecular basis of the pathobiology of lentiviruses.. Virus Res 1994 May;32(2):97-109.
          pubmed: 8067058doi: 10.1016/0168-1702(94)90037-xgoogle scholar: lookup
        6. Corn PG, McDonald ER 3rd, Herman JG, El-Deiry WS. Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein.. Nat Genet 2003 Nov;35(3):229-37.
          pubmed: 14556007doi: 10.1038/ng1254google scholar: lookup
        7. Covaleda L, Fuller FJ, Payne SL. EIAV S2 enhances pro-inflammatory cytokine and chemokine response in infected macrophages.. Virology 2010 Feb 5;397(1):217-23.
          pmc: PMC2813941pubmed: 19945727doi: 10.1016/j.virol.2009.11.005google scholar: lookup
        8. 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 May 25;349(1):22-30.
          pubmed: 16503341doi: 10.1016/j.virol.2005.12.041google scholar: lookup
        9. Hoyle J, Tan KH, Fisher EM. Localization of genes encoding two human one-domain members of the AAA family: PSMC5 (the thyroid hormone receptor-interacting protein, TRIP1) and PSMC3 (the Tat-binding protein, TBP1).. Hum Genet 1997 Feb;99(2):285-8.
          pubmed: 9048938doi: 10.1007/s004390050356google scholar: lookup
        10. Jansen BJ, Eleveld-Trancikova D, Sanecka A, van Hout-Kuijer M, Hendriks IA, Looman MG, Leusen JH, Adema GJ. OS9 interacts with DC-STAMP and modulates its intracellular localization in response to TLR ligation.. Mol Immunol 2009 Feb;46(4):505-15.
          pubmed: 18952287doi: 10.1016/j.molimm.2008.06.032google scholar: lookup
        11. Kimura Y, Nakazawa M, Yamada M. Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines.. J Biochem 1998 May;123(5):876-82.
          pubmed: 9562620doi: 10.1093/oxfordjournals.jbchem.a022019google scholar: lookup
        12. Krummheuer J, Johnson AT, Hauber I, Kammler S, Anderson JL, Hauber J, Purcell DF, Schaal H. A minimal uORF within the HIV-1 vpu leader allows efficient translation initiation at the downstream env AUG.. Virology 2007 Jul 5;363(2):261-71.
          pubmed: 17331561doi: 10.1016/j.virol.2007.01.022google scholar: lookup
        13. Lassot I, Latreille D, Rousset E, Sourisseau M, Linares LK, Chable-Bessia C, Coux O, Benkirane M, Kiernan RE. The proteasome regulates HIV-1 transcription by both proteolytic and nonproteolytic mechanisms.. Mol Cell 2007 Feb 9;25(3):369-83.
          pubmed: 17289585doi: 10.1016/j.molcel.2006.12.020google scholar: lookup
        14. 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 Jan;74(1):573-9.
          pmc: PMC111574pubmed: 10590152doi: 10.1128/jvi.74.1.573-579.2000google scholar: lookup
        15. Li F, Puffer BA, Montelaro RC. The S2 gene of equine infectious anemia virus is dispensable for viral replication in vitro.. J Virol 1998 Oct;72(10):8344-8.
          pmc: PMC110207pubmed: 9733881doi: 10.1128/jvi.72.10.8344-8348.1998google scholar: lookup
        16. Litovchick L, Friedmann E, Shaltiel S. A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta.. J Biol Chem 2002 Sep 13;277(37):34413-23.
          pubmed: 12093806doi: 10.1074/jbc.m203986200google scholar: lookup
        17. Malim MH, Emerman M. HIV-1 accessory proteins--ensuring viral survival in a hostile environment.. Cell Host Microbe 2008 Jun 12;3(6):388-98.
          pubmed: 18541215doi: 10.1016/j.chom.2008.04.008google scholar: lookup
        18. Montelaro RC, Ball JM, Rushlow KE. Equine retroviruses. The Retroviridae Vol. 2. Plenum Press; New York and London: 1993. pp. 257–360.
        19. Nelbock P, Dillon PJ, Perkins A, Rosen CA. A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator.. Science 1990 Jun 29;248(4963):1650-3.
          pubmed: 2194290doi: 10.1126/science.2194290google scholar: lookup
        20. Payne S, Lim WS, Fuller FJ, Ball JM. Equine infectious anemia virus as a model for lentiviral pathogenesis. Vivo Models of HIV Disease and Control Springer; New York: 2006. pp. 365–390.
        21. Rozan LM, El-Deiry WS. Identification and characterization of proteins interacting with Traf4, an enigmatic p53 target.. Cancer Biol Ther 2006 Sep;5(9):1228-35.
          pubmed: 16969126doi: 10.4161/cbt.5.9.3295google scholar: lookup
        22. Satoh T, Ishizuka T, Tomaru T, Yoshino S, Nakajima Y, Hashimoto K, Shibusawa N, Monden T, Yamada M, Mori M. Tat-binding protein-1 (TBP-1), an ATPase of 19S regulatory particles of the 26S proteasome, enhances androgen receptor function in cooperation with TBP-1-interacting protein/Hop2.. Endocrinology 2009 Jul;150(7):3283-90.
          pmc: PMC2703560pubmed: 19325002doi: 10.1210/en.2008-1122google scholar: lookup
        23. Schiltz RL, Shih DS, Rasty S, Montelaro RC, Rushlow KE. Equine infectious anemia virus gene expression: characterization of the RNA splicing pattern and the protein products encoded by open reading frames S1 and S2.. J Virol 1992 Jun;66(6):3455-65.
          pmc: PMC241126pubmed: 1316461doi: 10.1128/jvi.66.6.3455-3465.1992google scholar: lookup
        24. Schwartz S, Felber BK, Pavlakis GN. Mechanism of translation of monocistronic and multicistronic human immunodeficiency virus type 1 mRNAs.. Mol Cell Biol 1992 Jan;12(1):207-19.
          pmc: PMC364085pubmed: 1729599doi: 10.1128/mcb.12.1.207-219.1992google scholar: lookup
        25. Su YA, Hutter CM, Trent JM, Meltzer PS. Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas.. Mol Carcinog 1996 Apr;15(4):270-5.
          pubmed: 8634085doi: 10.1002/(sici)1098-2744(199604)15:4<270::aid-mc4>3.0.co;2-kgoogle scholar: lookup
        26. Tanahashi N, Suzuki M, Fujiwara T, Takahashi E, Shimbara N, Chung CH, Tanaka K. Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases.. Biochem Biophys Res Commun 1998 Feb 4;243(1):229-32.
          pubmed: 9473509doi: 10.1006/bbrc.1997.7892google scholar: lookup
        27. Truax AD, Koues OI, Mentel MK, Greer SF. The 19S ATPase S6a (S6'/TBP1) regulates the transcription initiation of class II transactivator.. J Mol Biol 2010 Jan 15;395(2):254-69.
          pubmed: 19853614doi: 10.1016/j.jmb.2009.10.035google scholar: lookup
        28. Wang Y, Fu X, Gaiser S, Köttgen M, Kramer-Zucker A, Walz G, Wegierski T. OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum.. J Biol Chem 2007 Dec 14;282(50):36561-70.
          pubmed: 17932042doi: 10.1074/jbc.m703903200google scholar: lookup
        29. Yoon S, Kingsman SM, Kingsman AJ, Wilson SA, Mitrophanous KA. Characterization of the equine infectious anaemia virus S2 protein.. J Gen Virol 2000 Sep;81(Pt 9):2189-2194.
          pubmed: 10950976doi: 10.1099/0022-1317-81-9-2189google scholar: lookup

        Citations

        This article has been cited 5 times.
        1. Li M, Waheed AA, Yu J, Zeng C, Chen HY, Zheng YM, Feizpour A, Reinhard BM, Gummuluru S, Lin S, Freed EO, Liu SL. TIM-mediated inhibition of HIV-1 release is antagonized by Nef but potentiated by SERINC proteins. Proc Natl Acad Sci U S A 2019 Mar 19;116(12):5705-5714.
          doi: 10.1073/pnas.1819475116pubmed: 30842281google scholar: lookup
        2. 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 U S A 2016 Nov 15;113(46):13197-13202.
          doi: 10.1073/pnas.1612044113pubmed: 27803322google scholar: lookup
        3. Wang XF, Wang S, Liu Q, Lin YZ, Du C, Tang YD, Na L, Wang X, Zhou JH. A unique evolution of the s2 gene of equine infectious anemia virus in hosts correlated with particular infection statuses. Viruses 2014 Nov 10;6(11):4265-79.
          doi: 10.3390/v6114265pubmed: 25390683google scholar: lookup
        4. Ma Y, Wang C, Li B, Qin L, Su J, Yang M, He S. Bcl-2-associated transcription factor 1 interacts with fragile X-related protein 1. Acta Biochim Biophys Sin (Shanghai) 2014 Feb;46(2):119-27.
          doi: 10.1093/abbs/gmt134pubmed: 24389646google scholar: lookup
        5. 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
        Subscribe to our newsletter
        Join 99,000 horse owners like you who receive our email updates on horse health and nutrition.