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Home / Equine Research Bank / J Virol / Analysis of equine humoral immune responses to the transmemb...
Journal of virology1991; 65(2); 1013-1018; doi: 10.1128/JVI.65.2.1013-1018.1991

Analysis of equine humoral immune responses to the transmembrane envelope glycoprotein (gp45) of equine infectious anemia virus.

Abstract: Defined segments of the transmembrane envelope glycoprotein (gp45) of equine infectious anemia virus were expressed as TrpLE fusion proteins and examined for their reactivity in Western immunoblots against a diverse panel of equine immune sera. The most immunogenic region of gp45 was localized to its amino terminus, positioned between the hydrophobic fusion and the transmembrane domains. A series of overlapping synthetic peptides were used in enzyme-linked immunosorbent assays to define an immunodominant epitope within this region. In contrast, the carboxy-terminal half of gp45 displayed both weak and variable immunoreactivity with equine immune sera.
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Publication Date: 1991-02-01 PubMed ID: 1846180PubMed Central: PMC239850DOI: 10.1128/JVI.65.2.1013-1018.1991Google Scholar: Lookup
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  • Journal Article
  • 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.

This research investigates the immune response of horses to the gp45 envelope protein of the equine infectious anemia virus (EIAV). The study found that out of the parts of gp45 analyzed, the area located at the beginning of the protein, between its fusion and transmembrane domains, aroused the strongest response from the equine immune system.

Study Methodology

  • The research involved using distinct segments of the gp45 envelope protein from the EIAV.
  • The segments were expressed as TrpLE fusion proteins. Fusion proteins are created through genetic engineering, combining properties of multiple proteins for analysis.
  • These proteins were then studied using Western immunoblotting against a varied panel of equine immune sera. This technique allows scientists to identify specific proteins within a complex sample based on their immune reactivity.

Key Findings

  • The most immunogenic area of the gp45 protein, meaning the region that elicits the strongest immune response, was found to be localized at the amino terminus. This is the starting end of the protein, positioned between the hydrophobic fusion and transmembrane domains.
  • To better define an immunodominant epitope within this highly reactive region, a series of overlapping synthetic peptides were used in enzyme-linked immunosorbent assays. An epitope is the portion of an antigen that is recognized and bound by an antibody, while the assay in question is a common laboratory technique designed to measure antibodies in a sample.
  • The research found that the carboxy-terminal half of gp45, the end area of the protein, resulted in both weak and inconsistent immunoreactivity with equine immune sera. This suggests it is not a potent target for the equine immune system.

Significance of the Research

  • Understanding the immune response to various parts of EIAV assists in furthering knowledge about the virus itself, as well as potential vaccine targets.
  • This research points out immunodominant regions on the EIAV, which are crucial to consider in the development of effective vaccines or therapies.

Cite This Article

APA
Chong YH, Ball JM, Issel CJ, Montelaro RC, Rushlow KE. (1991). Analysis of equine humoral immune responses to the transmembrane envelope glycoprotein (gp45) of equine infectious anemia virus. J Virol, 65(2), 1013-1018. https://doi.org/10.1128/JVI.65.2.1013-1018.1991

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 65
Issue: 2
Pages: 1013-1018

Researcher Affiliations

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

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Antibody Formation
          • Cell Membrane / ultrastructure
          • DNA, Viral / genetics
          • Equine Infectious Anemia / immunology
          • Genes, Viral
          • Horses / immunology
          • Immune Sera / immunology
          • Infectious Anemia Virus, Equine / genetics
          • Infectious Anemia Virus, Equine / immunology
          • Models, Structural
          • Molecular Sequence Data
          • Protein Conformation
          • Recombinant Fusion Proteins / immunology
          • Restriction Mapping
          • Viral Envelope Proteins / genetics
          • Viral Envelope Proteins / immunology

          Grant Funding

          • 1R01-AI25850 / NIAID NIH HHS

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          Citations

          This article has been cited 11 times.
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