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Home / Equine Research Bank / J Virol / Sequence conservation and antigenic variation of the structu...
Journal of virology2001; 75(21); 10550-10556; doi: 10.1128/JVI.75.21.10550-10556.2001

Sequence conservation and antigenic variation of the structural proteins of equine rhinitis A virus.

Abstract: The nucleotide and deduced amino acid sequences of the P1 region of the genomes of 10 independent equine rhinitis A virus (ERAV) isolates were determined and found to be very closely related. A panel of seven monoclonal antibodies to the prototype virus ERAV.393/76 that bound to nonneutralization epitopes conserved among all 10 isolates was raised. In serum neutralization assays, rabbit polyclonal sera and sera from naturally and experimentally infected horses reacted in a consistent and discriminating manner with the 10 isolates, which indicated the existence of variation in the neutralization epitopes of these viruses.
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Publication Date: 2001-10-03 PubMed ID: 11581430PubMed Central: PMC114636DOI: 10.1128/JVI.75.21.10550-10556.2001Google Scholar: Lookup
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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 examined the genetic and protein differences in 10 separate samples of equine rhinitis A virus (ERAV), finding significant similarity across samples, but also distinct variation that affects virus neutralization.

Overview

  • This study focused on determining the nucleotide and amino acid sequences of the P1 region (part of a virus’s genome) in 10 separate isolates of the equine rhinitis A virus (ERAV), a common virus causing respiratory disease in horses.
  • The researchers found that the sequences in these isolates were very closely related, showing a high degree of sequence conservation among different isolates of the ERAV.

Monoclonal Antibodies

  • The researchers then raised a panel of seven monoclonal antibodies, which are lab-produced antibodies designed to bind to a specific antigen. In this case, they were produced to bind with the prototype virus ERAV.393/76.
  • The antibodies were observed to bind to nonneutralization epitopes, or parts of an antigen that don’t result in neutralization of the virus, conserved among all 10 isolates. This means that there were parts of the virus these antibodies could bind to that remained consistent across all isolates.

Serum Neutralization Assays

  • Serum neutralization assays, tests that measure the ability of serum to neutralize a virus, were then conducted using rabbit polyclonal sera and sera from horses that were either naturally infected with ERAV or had been experimentally infected as part of the study.
  • Despite the high degree of similarity found in the viral sequences, these assays revealed existence of variation in the neutralization epitopes of the viruses. This means the part of the virus that, when bound by an antibody, results in its neutralization, differs among the 10 isolates, which could affect virus neutralization.
  • This confirms the antigenic variation among different isolates of the virus, meaning they have different antigen structures capable of eliciting an immune response.

Cite This Article

APA
Varrasso A, Drummer HE, Huang JA, Stevenson RA, Ficorilli N, Studdert MJ, Hartley CA. (2001). Sequence conservation and antigenic variation of the structural proteins of equine rhinitis A virus. J Virol, 75(21), 10550-10556. https://doi.org/10.1128/JVI.75.21.10550-10556.2001

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 75
Issue: 21
Pages: 10550-10556

Researcher Affiliations

Varrasso, A
  • Centre for Equine Virology, School of Veterinary Science, The University of Melbourne, Parkville, Victoria 3010, Australia.
Drummer, H E
    Huang, J A
      Stevenson, R A
        Ficorilli, N
          Studdert, M J
            Hartley, C A

              MeSH Terms

              • Amino Acid Sequence
              • Animals
              • Antibodies, Monoclonal / immunology
              • Aphthovirus / chemistry
              • Aphthovirus / classification
              • Aphthovirus / immunology
              • Capsid / chemistry
              • Capsid / immunology
              • Capsid Proteins
              • Conserved Sequence
              • Epitopes
              • Horses / virology
              • Molecular Sequence Data
              • Phylogeny
              • Rabbits

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              Citations

              This article has been cited 2 times.
              1. Tuthill TJ, Harlos K, Walter TS, Knowles NJ, Groppelli E, Rowlands DJ, Stuart DI, Fry EE. Equine rhinitis A virus and its low pH empty particle: clues towards an aphthovirus entry mechanism?. PLoS Pathog 2009 Oct;5(10):e1000620.
                doi: 10.1371/journal.ppat.1000620pubmed: 19816570google scholar: lookup
              2. Li F, Stevenson RA, Crabb BS, Studdert MJ, Hartley CA. Several recombinant capsid proteins of equine rhinitis a virus show potential as diagnostic antigens.. Clin Diagn Lab Immunol 2005 Jun;12(6):778-85.
                doi: 10.1128/CDLI.12.6.778-785.2005pubmed: 15939754google scholar: lookup
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