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Related Experiment Videos

Equine rhinitis A virus: structural proteins and immune response.

Carol A Hartley1, Nino Ficorilli1, Kemperly Dynon1

  • 1Centre for Equine Virology, School of Veterinary Science, The University of Melbourne, Parkville, Victoria 3010, Australia1.

The Journal of General Virology
|June 20, 2001
PubMed
Summary

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Equine rhinitis A virus (ERAV), a member of the Aphthovirus genus, shows specific cleavage sites in its capsid proteins. Antibody responses in horses and rabbits varied, correlating with reactivity to the VP1 protein.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Equine rhinitis A virus (ERAV) is a picornavirus recently reclassified into the Aphthovirus genus.
  • ERAV shares genomic similarities with foot-and-mouth disease virus.

Purpose of the Study:

  • To determine the N-terminal amino acid sequence of ERAV capsid proteins.
  • To investigate the proteolytic cleavage sites within the ERAV precursor P1 polypeptide.
  • To compare the reactivity of equine and rabbit antisera to ERAV structural proteins.

Main Methods:

  • N-terminal amino acid sequencing of ERAV capsid proteins.
  • Analysis of proteolytic and autocatalytic cleavage sites.
  • Serum neutralization assays.
  • Western blot analysis using ERAV antisera.

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Main Results:

  • Proteolytic cleavage sites within the P1 polypeptide were consistent with aphthovirus-like 3C protease activity, generating VP1 and VP3.
  • The autocatalytic cleavage site between VP4 and VP2 differed from previous predictions.
  • Equine and rabbit antisera exhibited distinct reactivity patterns against viral structural proteins.
  • High neutralizing antibody titers correlated with strong Western blot reactivity to VP1.

Conclusions:

  • ERAV processing of capsid proteins involves aphthovirus-like 3C protease and a distinct autocatalytic cleavage mechanism.
  • Antibody responses to ERAV are protein-specific, with VP1 being a key target for neutralizing antibodies.