Mapping epitopes in equine rhinitis A virus VP1 recognized by antibodies elicited in response to infection of the natural host

J Gen Virol. 2003 Jun;84(Pt 6):1607-1612. doi: 10.1099/vir.0.18848-0.

Abstract

Equine rhinitis A virus (ERAV) is an important respiratory pathogen of horses and is of additional interest because of its close relationship and common classification with foot-and-mouth disease virus (FMDV). As is the case with FMDV, the VP1 capsid protein of ERAV has been shown to be a target of neutralizing antibodies. In FMDV VP1, such antibodies commonly recognize linear epitopes present in the betaG-betaH loop region. To map linear B cell epitopes in ERAV VP1, overlapping fragments spanning its length were expressed in Escherichia coli as glutathione S-transferase (GST) fusion proteins. These fusion proteins were tested for reactivity with sera from ERAV-infected horses and with polyclonal sera from ERAV-immunized rabbits and mice. Regions at the N- and C-termini as well as the betaE-betaF and the betaG-betaH loop regions contained B cell epitopes that elicited antibodies in the natural host. GST fusion proteins of these regions also elicited antibodies following immunization of rabbits and mice, which, in general, strongly recognized native ERAV VP1 but which were non-neutralizing. It is concluded that the N-terminal region of ERAV VP1, in particular, contains strong B cell epitopes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Viral
  • Antigens, Viral* / genetics
  • Aphthovirus / genetics
  • Aphthovirus / immunology*
  • Aphthovirus / pathogenicity
  • Capsid Proteins / genetics
  • Capsid Proteins / immunology*
  • Epitope Mapping
  • Horse Diseases / immunology
  • Horse Diseases / virology
  • Horses
  • Molecular Sequence Data
  • Picornaviridae Infections / immunology
  • Picornaviridae Infections / veterinary
  • Picornaviridae Infections / virology
  • Rabbits
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / immunology

Substances

  • Antibodies, Viral
  • Antigens, Viral
  • Capsid Proteins
  • Recombinant Fusion Proteins