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Home / Equine Research Bank / J Virol / Detailed mapping of the antigenicity of the surface unit gly...
Journal of virology1992; 66(2); 732-742; doi: 10.1128/JVI.66.2.732-742.1992

Detailed mapping of the antigenicity of the surface unit glycoprotein of equine infectious anemia virus by using synthetic peptide strategies.

Abstract: We describe here a detailed analysis of the antigenic determinants of the surface unit glycoprotein (gp90) of equine infectious anemia virus (EIAV), using a comprehensive panel of synthetic peptides in enzyme-linked immunosorbent assays with immune serum from naturally and experimentally infected horses and with a panel of gp90-specific neutralizing and nonneutralizing monoclonal antibodies. The results of these studies identify immunoreactive segments throughout the conserved and variable domains of gp90 but localize immunodominant (100% reactivity) determinants to the amino and carboxyl termini of the glycoprotein molecule. Analysis of peptide reactivities with longitudinal serum samples taken from experimentally infected ponies revealed that antibody responses to conserved B-cell determinants appeared earlier and at higher titers than do antibodies specific for determinants contained in the variable domain of gp90. These observations suggest an evolution of antibody responses in EIAV-infected ponies that may correspond to the establishment of immunological control of virus replication and disease routinely observed in EIAV infections. In addition, the mapping of monoclonal antibody epitopes to peptides of 9 to 12 amino acids demonstrated that all of the neutralizing epitopes are located in the variable domain of gp90. The arrangement of neutralizing epitopes and critical structural considerations suggest that EIAV gp90 contains a principal neutralizing domain similar to the V3 loop of human immunodeficiency virus type 1. These antigenic analyses provide an important foundation for further analyzing the protective immune response generated during persistent EIAV infections and also provide potential peptide substrates for diagnostic assays and for vaccine strategies.
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Publication Date: 1992-02-01 PubMed ID: 1370556PubMed Central: PMC240772DOI: 10.1128/JVI.66.2.732-742.1992Google Scholar: Lookup
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  • Research Support
  • U.S. Gov't
  • P.H.S.

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 presents a comprehensive mapping of the antigenic properties of a key protein related to Equine Infectious Anemia virus (EIAV). The researchers used different techniques and antibodies to identify the protein sequences that lead to immune responses.

Research Objectives and Methods

  • The study aimed to analyze the antigenic properties of the surface unit glycoprotein (gp90) of the EIAV.
  • Various synthetic peptides were used as part of enzyme-linked immunosorbent assays (ELISA).
  • The assays were performed using immune serum from horses that were naturally and experimentally infected with EIAV, allowing researchers to identify key segments that react with the immune system.

Results and Findings

  • The research identified immunoreactive segments throughout the conserved and variable domains of gp90, but found that immunodominant determinants (segments that caused the greatest reactivity) were located at the amino and carboxyl termini of the glycoprotein molecule.
  • Longitudinal serum samples from experimentally infected ponies revealed that the immune response towards the conserved B-cell antigens happens earlier and at a higher concentration than the response towards the variable domain of gp90.
  • All of the neutralizing epitopes (segments of the glycoprotein that cause the immune system to respond) were located in the variable domain of gp90.

Implications and Significance

  • This research suggests that the immune response in EIAV-infected ponies gradually develops, potentially corresponding to the establishment of immunological control of virus replication and routinely observed disease progression in EIAV infections.
  • The mapped gp90 glycoprotein could also have a similar principal neutralizing domain compared to the V3 loop of the human immunodeficiency virus type 1—an important finding given the pathogenic similarity between HIV in humans and EIAV in horses.
  • The findings provide a fundamental basis for further analysis of the protective immune response during persistent EIAV infections and also aim to improve the accuracy of diagnostic assays and allow for better vaccine strategies.

Cite This Article

APA
Ball JM, Rushlow KE, Issel CJ, Montelaro RC. (1992). Detailed mapping of the antigenicity of the surface unit glycoprotein of equine infectious anemia virus by using synthetic peptide strategies. J Virol, 66(2), 732-742. https://doi.org/10.1128/JVI.66.2.732-742.1992

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 66
Issue: 2
Pages: 732-742

Researcher Affiliations

Ball, J M
  • Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pennsylvania 15261.
Rushlow, K E
    Issel, C J
      Montelaro, R C

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Antibodies, Monoclonal
        • Enzyme-Linked Immunosorbent Assay
        • Epitopes / analysis
        • Equine Infectious Anemia / immunology
        • Equine Infectious Anemia / microbiology
        • Horses
        • Infectious Anemia Virus, Equine / immunology
        • Infectious Anemia Virus, Equine / isolation & purification
        • Infectious Anemia Virus, Equine / pathogenicity
        • Membrane Glycoproteins / analysis
        • Membrane Glycoproteins / immunology
        • Models, Structural
        • Molecular Sequence Data
        • Peptides / chemical synthesis
        • Peptides / immunology
        • Protein Conformation
        • Viral Proteins / analysis
        • Viral Proteins / immunology
        • Virulence

        Grant Funding

        • R0I-AI25850 / NIAID NIH HHS

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