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Virus research1995; 39(2-3); 277-288; doi: 10.1016/0168-1702(95)00098-4

Expression cloning and antigenic analysis of the nucleocapsid protein of equine arteritis virus.

Abstract: A series of recombinant fusion proteins derived from equine arteritis virus (EAV) open reading frame (ORF) 7 have been used to define the immunoreactive region of the viral nucleocapsid (N) protein. Reactivities of recombinant N fusion proteins with post-infection equine sera in immunoblots and ELISAs indicate that the major nucleocapsid protein epitope is located within amino acid residues 1-69. In ELISAs two recombinant nucleocapsid fusion proteins containing residues 1-69 (rN1-69) and 1-28 (rN1-28) discriminated between pre- and post-infection, and pre- and post-vaccination serum samples. Additionally rN1-69 and rN1-28 detected seroconversions following vaccination with a killed virus preparation, even in the absence of a detectable virus neutralising response. Although a good correlation existed between virus neutralising antibody and rN1-69 ELISA positive values in post-infection sera, all the rN proteins failed to induce any virus neutralising response in immunised rabbits.
Publication Date: 1995-12-01 PubMed ID: 8837890PubMed Central: PMC7133929DOI: 10.1016/0168-1702(95)00098-4Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research focuses on identifying the main immune-recognized region of the nucleocapsid protein of the equine arteritis virus (EAV) through the use of recombinant fusion proteins. The study finds that this region is located within the first 69 amino acid residues of the protein and is able to differentiate between pre- and post-infection as well as vaccination serum samples.

Concept of the Research

  • The study is centered on the equine arteritis virus (EAV), a virus that affects horses. The researchers specifically look at the nucleocapsid (N) protein of the virus. The N protein is a viral protein associated with the genetic material of the virus.
  • The study uses recombinant fusion proteins, which are proteins created through genetic engineering, to determine important aspects of the N protein. In this case, the recombinant proteins are derived from EAV’s open reading frame (ORF) 7, a part of the virus’ genetic material that can be translated into proteins.

Findings of the Research

  • The researchers discovered that the main epitope, or part of the antigen that is recognized by the immune system, of the N protein is located within the first 69 amino acid residues. Amino acids are the building blocks of proteins and an “amino acid residue” refers to a single amino acid in a peptide chain.
  • In enzyme-linked immunosorbent assays (ELISAs), two recombinant N fusion proteins containing the first 69 (rN1-69) and 28 (rN1-28) residues could differentiate between pre- and post-infection and pre- and post-vaccination serum samples. This suggests these proteins could potentially be used as diagnostic tools.
  • The rN1-69 and rN1-28 proteins could also detect a change in the immune response (seroconversion) following vaccination, even if there was no detectable virus-neutralising response.

Significance of the Research

  • Despite successfully identifying the major nucleocapsid protein epitope, the researchers found that all the recombinant N proteins used in the study failed to induce a virus-neutralizing response in vaccinated rabbits. A virus-neutralizing response refers to the immune system’s ability to inhibit virus infectivity.
  • This suggests that while these proteins could potentially serve as useful diagnostic tools, more research is needed to understand how they could be used in a therapeutic or preventative capacity against EAV.

Cite This Article

APA
Chirnside ED, Francis PM, Mumford JA. (1995). Expression cloning and antigenic analysis of the nucleocapsid protein of equine arteritis virus. Virus Res, 39(2-3), 277-288. https://doi.org/10.1016/0168-1702(95)00098-4

Publication

ISSN: 0168-1702
NlmUniqueID: 8410979
Country: Netherlands
Language: English
Volume: 39
Issue: 2-3
Pages: 277-288

Researcher Affiliations

Chirnside, E D
  • Centre for Preventive Medicine, Animal Health Trust, Newmarket, Suffolk, UK.
Francis, P M
    Mumford, J A

      MeSH Terms

      • Animals
      • Antigens, Viral / genetics
      • Antigens, Viral / immunology
      • Base Sequence
      • Cloning, Molecular
      • DNA Primers
      • Equartevirus / genetics
      • Equartevirus / immunology
      • Gene Expression Regulation, Viral
      • Horses
      • Immune Sera / immunology
      • Molecular Sequence Data
      • Nucleocapsid / genetics
      • Nucleocapsid / immunology
      • Rabbits
      • Recombinant Fusion Proteins / genetics
      • Recombinant Fusion Proteins / immunology

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