Analyze Diet
Acta veterinaria Hungarica2008; 56(2); 265-270; doi: 10.1556/AVet.56.2008.2.14

Denatured virion protein 1 of equine rhinitis B virus 1 contains authentic B-cell epitopes recognised in an enzyme-linked immunosorbent assay–short communication.

Abstract: Equine rhinitis B virus 1 (ERBV1), genus Erbovirus, family Picornaviridae, is a pathogen of horses which causes clinical and subclinical infection of the upper respiratory tract in horses. The virus is widespread in European horse populations and the current standard method for the detection of antibody against ERBV1 is by virus neutralisation (VN). VN tests, however, are labour-intensive and time-consuming, require tissue culture facilities, and generally do not provide same-day results. In this study, a protocol for the high-level expression and purification of recombinant virion protein 1 (rVP1) was established using metal-chelate affinity chromatography under denaturing condition. When used as a coating antigen in a prototype enzyme-linked immunosorbent assay (ELISA), denatured rVP1 was recognised by ERBV1 antibody present in horse serum. This finding suggests that denatured rVP1 is a promising candidate for the development of an ELISA to be used in the routine laboratory diagnosis of ERBV1 infection in horses.
Publication Date: 2008-08-02 PubMed ID: 18669254DOI: 10.1556/AVet.56.2008.2.14Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
  • 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 research involved the development of a faster, more efficient method for diagnosing equine rhinitis B virus 1 (ERBV1) in horses. They successfully created a protocol to enhance the expression of the virus’ protein, which can be utilized in an enzyme-linked immunosorbent assay (ELISA).

Background

  • ERBV1 belongs to the genus Erbovirus within the Picornaviridae family. It causes both clinical and subclinical infections in the upper respiratory tract of horses.
  • The virus is common among European horse populations. The traditional method used to detect the ERBV1 antibody is through virusneutralisation (VN). However, this method has several drawbacks such as its labor intensiveness, time-consuming nature, the necessity for tissue culture facilities, and it doesn’t deliver same-day results.

Study Objective

  • The primary aim of the study was to establish a faster and more convenient protocol for the detection of ERBV1. To achieve this, the researchers aimed to amplify and purify a recombinant form of the virion protein 1 (rVP1) related to the virus.

Methodology

  • The researchers developed a method to express and purify recombinant virion protein 1 (rVP1) in larger amounts through metal-chelate affinity chromatography conducted under denaturing conditions.
  • This rVP1 was then utilized as a coating antigen in a prototype ELISA. The process of denaturing rVP1 does not hinder its recognition by the ERBV1 antibodies present in horse serum.

Findings and Conclusion

  • Summarily, the use of denatured rVP1 in the ELISA proved successful, as it was recognized by the ERBV1 antibodies within horse serum. This result indicates that denatured rVP1 could be a valuable antigen for developing an ELISA that can be utilized in the routine laboratory diagnosis of ERBV1 infections in horses.
  • This study not only contributes to easing the process of diagnosing ERBV1 but also presents an efficient method that can provide same-day test results, hence improving horse healthcare.

Cite This Article

APA
Kriegshäuser G, Cullinane A, Kuechler E, Skern T. (2008). Denatured virion protein 1 of equine rhinitis B virus 1 contains authentic B-cell epitopes recognised in an enzyme-linked immunosorbent assay–short communication. Acta Vet Hung, 56(2), 265-270. https://doi.org/10.1556/AVet.56.2008.2.14

Publication

ISSN: 0236-6290
NlmUniqueID: 8406376
Country: Hungary
Language: English
Volume: 56
Issue: 2
Pages: 265-270

Researcher Affiliations

Kriegshäuser, Gernot
  • Max F. Perutz Laboratories, Medical University of Vienna, Vienna, Austria. kriegshauser@viennalab.co.at
Cullinane, Anne
    Kuechler, Ernst
      Skern, Timothy

        MeSH Terms

        • Animals
        • Antibodies, Viral / blood
        • Antigens, Viral / chemistry
        • Enzyme-Linked Immunosorbent Assay / veterinary
        • Epitopes, B-Lymphocyte / analysis
        • Erbovirus / immunology
        • Erbovirus / isolation & purification
        • Horse Diseases / virology
        • Horses
        • Picornaviridae Infections / veterinary
        • Picornaviridae Infections / virology
        • Respiratory Tract Infections / veterinary
        • Respiratory Tract Infections / virology

        Citations

        This article has been cited 0 times.