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The Journal of general virology1994; 75 ( Pt 9); 2439-2444; doi: 10.1099/0022-1317-75-9-2439

Monoclonal antibodies to equine arteritis virus proteins identify the GL protein as a target for virus neutralization.

Abstract: Monoclonal antibodies (MAbs) to equine arteritis virus (EAV) proteins were produced and characterized. The protein specificities of eight MAbs were determined definitively by immunoprecipitation of EAV proteins expressed from vaccinia virus recombinants (VVRs). Included were two new VVRs produced for this study, expressing the M and the GL proteins, respectively. Three MAbs were determined to be N-specific and five MAbs recognized the GL protein. One GL-specific MAb, 17F5, of the IgA class, efficiently neutralized EAV infectivity. In competitive binding assays (CBAs), the N-specific MAbs defined a single antigenic domain on this protein. Four GL-specific MAbs, including MAb 17F5, demonstrated strong reciprocal competition in binding to the GL protein but differed in their virus-neutralizing ability. Thus the antigenic domain defined by these MAbs is probably composed of overlapping or closely adjacent epitopes. The fifth GL-specific MAb, a non-neutralizing antibody, may define an epitope adjacent to this antigenic domain as reciprocal CBAs demonstrated lower competition.
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Publication Date: 1994-09-01 PubMed ID: 8077945DOI: 10.1099/0022-1317-75-9-2439Google Scholar: Lookup
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  • Journal Article

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 study produced and characterized Monoclonal antibodies (MAbs) to equine arteritis virus (EAV) proteins, specifically identifying the GL protein as a prime target for virus neutralization.

Antibody Production and Determination of Specificities

  • The research team produced Monoclonal antibodies, which are antibodies derived from a single parental cell, to substances present in the equine arteritis virus (EAV). This virus is responsible for causing equine viral arteritis, a condition that can lead to respiratory illness and abortion in horses.
  • These antibodies were then characterized, and the protein specificities of eight Monoclonal antibodies were definitively determined through a process known as immunoprecipitation. In this process, immune materials such as antibodies are added to a solution to trigger a reaction that causes specific antigens (foreign substances in the body) to form visible clumps.
  • The proteins were expressed from vaccinia virus recombinants (VVRs), which are engineered viruses that contain genes or proteins from EAV. Two new VVRs were created for this study to express the M and GL proteins.

Identification of N-Specific and GL-Specific Antibodies

  • Three of the Monoclonal antibodies were found to be N-specific, meaning they target the N protein of the EAV. Five Monoclonal antibodies were determined to be GL-specific, targeting the GL protein.
  • One GL-specific Monoclonal antibody, named 17F5, and classified under the IgA class, was found to effectively neutralize the infectivity of EAV. Neutralizing antibodies inhibit or abolish the biological effect of the virus.

Understanding Antigenic Domains Through Competitive Binding Assays

  • In competitive binding assays, a technique used to evaluate binding affinities and interactions between molecules, it was discovered that the N-specific Monoclonal antibodies identified a single antigenic domain, or region that can interact with an antibody, on the N protein.
  • The four GL-specific Monoclonal antibodies exhibited strong reciprocal competition in binding to the GL proteins. This suggests that their respective areas of interest, or epitopes, are closely adjacent or overlapping on the antigenic domain of the GL protein.
  • Despite demonstrating competition in binding, these antibodies displayed varying levels of virus-neutralizing abilities.
  • The fifth GL-specific MAb, proposed to be a non-neutralizing antibody, potentially identifies an epitope close to the antigenic domain of the GL protein since it demonstrated lower competition in the binding assays.

Cite This Article

APA
Deregt D, de Vries AA, Raamsman MJ, Elmgren LD, Rottier PJ. (1994). Monoclonal antibodies to equine arteritis virus proteins identify the GL protein as a target for virus neutralization. J Gen Virol, 75 ( Pt 9), 2439-2444. https://doi.org/10.1099/0022-1317-75-9-2439

Publication

The Journal of general virology
ISSN: 0022-1317
NlmUniqueID: 0077340
Country: England
Language: English
Volume: 75 ( Pt 9)
Pages: 2439-2444

Researcher Affiliations

Deregt, D
  • Animal Diseases Research Institute, Agriculture Canada, Lethbridge, Alberta.
de Vries, A A
    Raamsman, M J
      Elmgren, L D
        Rottier, P J

          MeSH Terms

          • Animals
          • Antibodies, Monoclonal
          • Antibodies, Viral
          • Cell Line
          • Cricetinae
          • Electrophoresis, Polyacrylamide Gel
          • Equartevirus / immunology
          • GTP-Binding Proteins / analysis
          • GTP-Binding Proteins / immunology
          • Hybridomas
          • Kidney
          • Mice
          • Mice, Inbred BALB C / immunology
          • Neutralization Tests
          • Recombinant Proteins / biosynthesis
          • Recombinant Proteins / immunology
          • Recombinant Proteins / isolation & purification
          • Recombination, Genetic
          • Vaccinia virus
          • Viral Structural Proteins / biosynthesis
          • Viral Structural Proteins / immunology
          • Viral Structural Proteins / isolation & purification

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