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The Journal of general virology1995; 76 ( Pt 8); 1989-1998; doi: 10.1099/0022-1317-76-8-1989

Equine arteritis virus-neutralizing antibody in the horse is induced by a determinant on the large envelope glycoprotein GL.

Abstract: Complementary DNAs encoding ORFs 2 to 7 equine arteritis virus (EAV) have been cloned into the expression vector pGEX to produce glutathione-S-transferase fusion proteins. Recombinant proteins were affinity purified and screened in ELISA with equine sera to identify immunoreactive polypeptides. The large envelope glycoprotein (GL) was identified as the most reactive to EAV-positive equine sera and an immuno-dominant epitope was mapped between amino acids 55 and 98 by subcloning and expression. A fusion protein covering this region and a GL-specific synthetic peptide (residues 75 through 97) induced EAV-neutralizing antibody in vaccinated horses. The defined antigenic region of GL is likely to be exposed on the surface of the native EAV virion and consequently may be useful in the development of diagnostic tests and vaccines.
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Publication Date: 1995-08-01 PubMed ID: 7636479DOI: 10.1099/0022-1317-76-8-1989Google Scholar: Lookup
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  • 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.

This research discusses the identification of a key component in the equine arteritis virus (EAV) that causes a response in horse immune systems. It suggests that this component could be used for diagnostic tests and vaccines.

Introduction to the Research

  • The study focuses on identifying certain portions (ORFs 2 to 7) of the equine arteritis virus (EAV), a sexually transmitted disease in horses leading to various health issues like respiratory illness and abortion.
  • For the experiment, the researchers utilized complementary DNAs encoding the said ORFs and cloned them into an expression vector known as pGEX to produce fusion proteins.

Methodology and Process

  • These fusion proteins were then purified using an affinity purification technique, a method where targeted proteins are selectively isolated from a mixture, increasing the purity of the result.
  • The researchers applied an enzyme-linked immunosorbent assay (ELISA) using horse blood serum to these purified proteins. This test is used to detect and measure antibodies in blood and identify immunoreactive polypeptides or sections of the virus that causes an immune response.

Key Findings

  • The large envelope glycoprotein (GL), a component of EAV, appeared to be highly reactive to the horse’s immune systems.
  • Further analysis allowed the researchers to map an immuno-dominant epitope, a section of the protein that the immune system recognizes, between amino acids 55 and 98 of the GL protein.
  • A fusion protein covering this region and a GL-specific synthetic peptide (residues 75 through 97) caused the horse’s immune system to produce EAV-neutralizing antibodies when used as a vaccine.

Implications and Conclusions

  • This specific region of GL seems prone to exposure on the surface of the EAV virion or virus particle, making it a viable target for the immune system.
  • Thus, it may be used for diagnostic tests to identify EAV infection or to develop vaccines to combat EAV in horses.

Cite This Article

APA
Chirnside ED, de Vries AA, Mumford JA, Rottier PJ. (1995). Equine arteritis virus-neutralizing antibody in the horse is induced by a determinant on the large envelope glycoprotein GL. J Gen Virol, 76 ( Pt 8), 1989-1998. https://doi.org/10.1099/0022-1317-76-8-1989

Publication

The Journal of general virology
ISSN: 0022-1317
NlmUniqueID: 0077340
Country: England
Language: English
Volume: 76 ( Pt 8)
Pages: 1989-1998

Researcher Affiliations

Chirnside, E D
  • Department of Infectious Diseases, Animal Health Trust, Kennett, Newmarket, UK.
de Vries, A A
    Mumford, J A
      Rottier, P J

        MeSH Terms

        • Animals
        • Antibodies, Viral / biosynthesis
        • Base Sequence
        • Equartevirus / immunology
        • Glutathione Transferase / genetics
        • Horses
        • Immune Sera
        • Immunization
        • Immunization Schedule
        • Immunodominant Epitopes / immunology
        • Molecular Sequence Data
        • Neutralization Tests
        • Open Reading Frames / genetics
        • Peptide Fragments / chemical synthesis
        • Peptide Fragments / immunology
        • Rabbits
        • Recombinant Fusion Proteins / immunology
        • Viral Envelope Proteins / immunology

        Citations

        This article has been cited 20 times.
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        17. Chirnside ED, Francis PM, Mumford JA. Expression cloning and antigenic analysis of the nucleocapsid protein of equine arteritis virus. Virus Res 1995 Dec;39(2-3):277-88.
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        19. Mijnes JD, van der Horst LM, van Anken E, Horzinek MC, Rottier PJ, de Groot RJ. Biosynthesis of glycoproteins E and I of feline herpesvirus: gE-gI interaction is required for intracellular transport. J Virol 1996 Aug;70(8):5466-75.
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        20. Chirnside ED, Francis PM, de Vries AA, Sinclair R, Mumford JA. Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus. J Virol Methods 1995 Jul;54(1):1-13.
          doi: 10.1016/0166-0934(95)00020-upubmed: 7559853google scholar: lookup
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