Analyze Diet
Archives of virology2008; 153(2); 351-356; doi: 10.1007/s00705-007-1094-y

Characterization of equine arteritis virus particles and demonstration of their hemolytic activity.

Abstract: Equine arteritis virus (EAV), a member of the newly established family Arteriviridae, is a small, positive-stranded RNA virus. It carries two protein complexes in its envelope, gp5/M and the recently described gp2b/gp3/gp4 complex. We report here on several basic features of EAV replication in cell culture and on the protein composition of virus particles. We have also characterized gp2b, gp3, and gp4 expressed using a baculovirus system in insect cells. Finally, we provide evidence that EAV possess hemagglutinating and hemolytic activity. The hemolysis assay might be useful for determining which of the surface proteins carries the receptor-binding and membrane fusion activity of EAV.
Publication Date: 2008-02-04 PubMed ID: 18219439PubMed Central: PMC7086761DOI: 10.1007/s00705-007-1094-yGoogle 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.
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

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 study focuses on exploring the basic attributes of Equine arteritis virus (EAV) replication in cell culture and its protein composition, and finding evidence of its hemagglutinating and hemolytic activity which could potentially help understand which surface protein accounts for the receptor-binding and membrane fusion activity of EAV.

Understanding Equine arteritis virus (EAV)

  • EAV is a small, positive-stranded RNA virus and belongs to the newly established family Arteriviridae.
  • It contains two protein complexes in its envelope: gp5/M and gp2b/gp3/gp4 complex.

Characterizing EAV replication and protein composition

  • This research focuses on discovering the basic features associated with EAV replication in a controlled cell culture and analyzing the protein composition of the virus particles.
  • The study also characterizes specific proteins such as gp2b, gp3, and gp4 which were expressed using a baculovirus system in insect cells.

Hemolytic Activity of EAV

  • The research implies that EAV features hemagglutinating and hemolytic activity.
  • Hemagglutination refers to clumping of red blood cells while hemolysis refers to the breakdown of red blood cells.

Implication of Hemolytic Activity

  • The hemolytic activity of EAV might be used to identify the receptor-binding and membrane fusion activity of EAV.
  • This indicates that the surface proteins of EAV could play a crucial role in its binding to cell receptors and subsequent entry into the cell, leading to infection.
  • A hemolysis assay could be an applicable experimental setup for determining the functional domain of the virus particle that is responsible for receptor-binding and membrane fusion.

Cite This Article

APA
Veit M, Kabatek A, Tielesch C, Hermann A. (2008). Characterization of equine arteritis virus particles and demonstration of their hemolytic activity. Arch Virol, 153(2), 351-356. https://doi.org/10.1007/s00705-007-1094-y

Publication

ISSN: 0304-8608
NlmUniqueID: 7506870
Country: Austria
Language: English
Volume: 153
Issue: 2
Pages: 351-356

Researcher Affiliations

Veit, M
  • Department of Immunology and Molecular Biology, Veterinary Faculty, Free University Berlin, Berlin, Germany. mveit@zedat.fu-berlin.de
Kabatek, A
    Tielesch, C
      Hermann, A

        MeSH Terms

        • Animals
        • Baculoviridae
        • Cell Line
        • Chickens
        • Cricetinae
        • Electrophoresis, Polyacrylamide Gel
        • Equartevirus / chemistry
        • Equartevirus / pathogenicity
        • Equartevirus / physiology
        • Erythrocytes / virology
        • Hemagglutination
        • Hemolysis
        • Spodoptera
        • Viral Proteins / analysis
        • Virus Replication / physiology

        References

        This article includes 21 references
        1. Burnet FM. Haemolysis by Newcastle disease virus.. Nature 1949;164:1008.
          doi: 10.1038/1641008a0pubmed: 15396728google scholar: lookup
        2. de Vries AA, Chirnside ED, Horzinek MC, Rottier PJ. Structural proteins of equine arteritis virus.. J Virol 1992;66:6294–6303.
          pmc: PMC240121pubmed: 1328669
        3. de Vries AA, Post SM, Raamsman MJ, Horzinek MC, Rottier PJ. The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers.. J Virol 1995;69:4668–4674.
          pmc: PMC189270pubmed: 7609031
        4. de Vries AA, Raamsman MJ, van Dijk HA, Horzinek MC, Rottier PJ. The small envelope glycoprotein (GS) of equine arteritis virus folds into three distinct monomers and a disulfide-linked dimer.. J Virol 1995;69:3441–3448.
          pmc: PMC189056pubmed: 7745690
        5. Dobbe JC, van der Meer Y, Spaan WJ, Snijder EJ. Construction of chimeric arteriviruses reveals that the ectodomain of the major glycoprotein is not the main determinant of equine arteritis virus tropism in cell culture.. Virology 2001;288:283–294.
          doi: 10.1006/viro.2001.1074pubmed: 11601900google scholar: lookup
        6. Hedges JF, Balasuriya UB, MacLachlan NJ. The open reading frame 3 of equine arteritis virus encodes an immunogenic glycosylated, integral membrane protein.. Virology 1999;264:92–98.
          doi: 10.1006/viro.1999.9982pubmed: 10544133google scholar: lookup
        7. Huang RT, Rott R, Klenk HD. Influenza viruses cause hemolysis and fusion of cells.. Virology 1981;110:243–247.
          doi: 10.1016/0042-6822(81)90030-1pubmed: 7210509google scholar: lookup
        8. Hyllseth B. A plaque assay of equine arteritis virus in BHK-21 cells.. Arch Gesamte Virusforsch 1969;28:26–33.
          doi: 10.1007/BF01250842pubmed: 4988871google scholar: lookup
        9. Hyllseth B. Structural proteins of equine arteritis virus.. Arch Gesamte Virusforsch 1973;40:177–188.
          doi: 10.1007/BF01242536pubmed: 4633581google scholar: lookup
        10. Kubota T, Inaba Y, Uwatoko K, Akashi H, Fukunaga Y. Hemagglutination with equine arteritis virus.. J Vet Med Sci 1997;59:943–945.
          doi: 10.1292/jvms.59.943pubmed: 9362047google scholar: lookup
        11. Lamb RA, Paterson RG, Jardetzky TS. Paramyxovirus membrane fusion: lessons from the F and HN atomic structures.. Virology 2006;344:30–37.
          doi: 10.1016/j.virol.2005.09.007pmc: PMC7172328pubmed: 16364733google scholar: lookup
        12. Maeda T, Ohnishi S. Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes.. FEBS Lett 1980;122:283–287.
          doi: 10.1016/0014-5793(80)80457-1pubmed: 7202720google scholar: lookup
        13. Sano Y, Inaba Y, Uwatoko K, Kubota T, Asagoe T, Kanaya J, Pan IJ, Akashi H, Fukunaga Y. Effect of heparin on hemagglutination by equine arteritis virus.. J Vet Med Sci 1998;60:447–450.
          doi: 10.1292/jvms.60.447pubmed: 9592716google scholar: lookup
        14. Snijder EJ, Meulenberg JJ. The molecular biology of arteriviruses.. J Gen Virol 1998;79(Pt 5):961–979.
          pubmed: 9603311
        15. Snijder EJ, van Tol H, Pedersen KW, Raamsman MJ, de Vries AA. Identification of a novel structural protein of arteriviruses.. J Virol 1999;73:6335–6345.
          pmc: PMC112712pubmed: 10400725
        16. Vaananen P, Kaariainen L. Haemolysis by two alphaviruses: Semliki Forest and Sindbis virus.. J Gen Virol 1979;43:593–601.
          doi: 10.1099/0022-1317-43-3-593pubmed: 39116google scholar: lookup
        17. Verheije MH, Welting TJ, Jansen HT, Rottier PJ, Meulenberg JJ. Chimeric arteriviruses generated by swapping of the M protein ectodomain rule out a role of this domain in viral targeting.. Virology 2002;303:364–373.
          doi: 10.1006/viro.2002.1711pubmed: 12490397google scholar: lookup
        18. Wieringa R, de Vries AA, Raamsman MJ, Rottier PJ. Characterization of two new structural glycoproteins, GP(3) and GP(4), of equine arteritis virus.. J Virol 2002;76:10829–10840.
        19. Wieringa R, De Vries AA, Post SM, Rottier PJ. Intra- and intermolecular disulfide bonds of the GP2b glycoprotein of equine arteritis virus: relevance for virus assembly and infectivity.. J Virol 2003;77:12996–13004.
        20. Wieringa R, de Vries AA, Rottier PJ. Formation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus.. J Virol 2003;77:6216–6226.
        21. Wieringa R, de Vries AA, van der Meulen J, Godeke GJ, Onderwater JJ, van Tol H, Koerten HK, Mommaas AM, Snijder EJ, Rottier PJ. Structural protein requirements in equine arteritis virus assembly.. J Virol 2004;78:13019–13027.