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Home / Equine Research Bank / J Virol / Evidence that Equine rhinitis A virus VP1 is a target of neu...
Journal of virology2001; 75(19); 9274-9281; doi: 10.1128/JVI.75.19.9274-9281.2001

Evidence that Equine rhinitis A virus VP1 is a target of neutralizing antibodies and participates directly in receptor binding.

Abstract: Equine rhinitis A virus (ERAV) is a respiratory pathogen of horses and is classified as an Aphthovirus, the only non-Foot-and-mouth disease virus (FMDV) member of this genus. In FMDV, virion protein 1 (VP1) is a major target of protective antibodies and is responsible for viral attachment to permissive cells via an RGD motif located in a distal surface loop. Although both viruses share considerable sequence identity, ERAV VP1 does not contain an RGD motif. To investigate antibody and receptor-binding properties of ERAV VP1, we have expressed full-length ERAV VP1 in Escherichia coli as a glutathione S-transferase (GST) fusion protein (GST-VP1). GST-VP1 reacted specifically with antibodies present in serum from a rabbit immunized with purified ERAV virions and also in convalescent-phase sera from horses experimentally infected with ERAV. An antiserum raised in rabbits to GST-VP1 reacted strongly with viral VP1 and effectively neutralized ERAV infection in vitro. Using a flow cytometry-based binding assay, we found that GST-VP1, but not other GST fusion proteins, bound to cell surface receptors. This binding was reduced in a dose-dependent manner by the addition of purified ERAV virions, demonstrating the specificity of this interaction. A separate cell-binding assay also implicated GST-VP1 in receptor binding. Importantly, anti-GST-VP1 antibodies inhibited the binding of ERAV virions to Vero cells, suggesting that these antibodies exert their neutralizing effect by blocking viral attachment. Thus ERAV VP1, like its counterpart in FMDV, appears to be both a target of protective antibodies and involved directly in receptor binding. This study reveals the potential of recombinant VP1 molecules to serve as vaccines and diagnostic reagents for the control of ERAV infections.
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Publication Date: 2001-09-05 PubMed ID: 11533189PubMed Central: PMC114494DOI: 10.1128/JVI.75.19.9274-9281.2001Google Scholar: Lookup
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  • Non-U.S. Gov't

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 research article looks into the role of the VP1 protein in the Equine rhinitis A virus (ERAV), particularly its function as a target for neutralizing antibodies and its involvement in receptor binding. The experiment used GST-VP1, a VP1 protein expressed in Escherichia coli, and found it to bind specifically to cell surface receptors, confirming its crucial part in the infection process and suggesting its potential use as a component for vaccines and diagnostic reagents.

Background

  • The study begins by establishing the context, noting that ERAV is a respiratory pathogen impacting horses and is the only non-Foot-and-mouth disease virus (FMDV) in the Aphthovirus genus.
  • In FMDV, the VP1 protein is a primary target of protective antibodies which neutralize the virus and also aids the virus when connecting to permissive cells.
  • The difference between ERAV and FMDV is pointed out, as ERAV VP1 does not contain an RGD motif, which is important for virus-cell attachment in FMDV.

Methodology

  • The researchers cultivated full-length ERAV VP1 in the bacteria Escherichia coli to form a fusion protein called GST-VP1.
  • This protein was subjected to the antibodies from a rabbit immunized with purified ERAV virions and convalescent-phase sera from horses infected experimentally with ERAV.
  • The researchers then raised an antiserum in rabbits to GST-VP1, which reacted strongly with viral VP1 and was capable of neutralizing ERAV infection in a laboratory setting.
  • To explore the receptor-binding properties of ERAV VP1, a flow cytometry-based binding assay was employed, finding that GST-VP1 bound to cell surface receptors.

Results

  • The GST-VP1 displayed specific binding to cell surface receptors, and when doses of purified ERAV virions were added, this binding decreased, showing the specificity of the interaction.
  • Another assay suggested that GST-VP1 has a role in receptor binding as well.
  • Critical to the study’s conclusion, antibodies against GST-VP1 prevented ERAV virions from binding to Vero cells, implying these antibodies impeded viral attachment and thus could neutralize the virus.

Conclusion

  • This study suggests that ERAV VP1 behaves much like its counterpart in FMDV, acting as a target for protective antibodies and participating directly in receptor binding.
  • Notably, it puts forward the potential use of recombinant VP1 molecules as vaccines or diagnostic tools for managing ERAV infections.

Cite This Article

APA
Warner S, Hartley CA, Stevenson RA, Ficorilli N, Varrasso A, Studdert MJ, Crabb BS. (2001). Evidence that Equine rhinitis A virus VP1 is a target of neutralizing antibodies and participates directly in receptor binding. J Virol, 75(19), 9274-9281. https://doi.org/10.1128/JVI.75.19.9274-9281.2001

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 75
Issue: 19
Pages: 9274-9281

Researcher Affiliations

Warner, S
  • Department of Microbiology and Immunology and the Co-Operative Research Centre for Vaccine Technology, The University of Melbourne, Victoria 3010, Australia.
Hartley, C A
    Stevenson, R A
      Ficorilli, N
        Varrasso, A
          Studdert, M J
            Crabb, B S

              MeSH Terms

              • Animals
              • Antibodies, Viral / immunology
              • Antibody Specificity
              • Capsid / immunology
              • Capsid Proteins
              • Chlorocebus aethiops
              • Picornaviridae / physiology
              • Picornaviridae Infections / immunology
              • Picornaviridae Infections / virology
              • Rabbits
              • Receptors, Virus / immunology
              • Vero Cells
              • Viral Proteins / immunology
              • Virus Replication

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