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Model of the equine rhinitis A virus capsid: identification of a major neutralizing immunogenic site

Gernot Kriegshäuser1, Gordana Wutz1, Susan Lea2

  • 1Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Department of Medical Biochemistry, Division of Biochemistry, University of Vienna, Dr Bohr Gasse 9/3, A-1030 Vienna, Austria.

The Journal of General Virology
|August 15, 2003
PubMed

Insights

Researchers identified key mutations in equine rhinitis A virus (ERAV) capsid protein VP1 conferring antibody resistance. These changes suggest a unique, complex immunogenic site formed by interacting VP1 regions.

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Equine rhinitis A virus (ERAV) causes significant respiratory illness in horses.
  • Understanding ERAV's antigenic structure is crucial for vaccine development and control strategies.
  • Neutralization escape mutants can reveal critical regions of viral proteins targeted by antibodies.

Purpose of the Study:

  • To identify the specific amino acid changes in ERAV responsible for resistance to neutralizing monoclonal antibodies (mAbs).
  • To elucidate the structural basis of the identified immunogenic site on the ERAV capsid protein VP1.
  • To compare the ERAV immunogenic site with that of related viruses, such as foot-and-mouth disease virus (FMDV).

Main Methods:

  • Selection and characterization of neutralization escape mutants of ERAV using mouse monoclonal antibodies (mAbs).
  • Amino acid sequencing of the capsid protein VP1 in the identified escape mutants.
  • Construction of a three-dimensional structural model of the ERAV capsid based on homology with FMDV.

Main Results:

  • Specific amino acid substitutions at Lys-114, Pro-240, and Thr-241 in VP1 conferred resistance to neutralization.
  • These mutants exhibited cross-resistance to all four mAbs, indicating a single, conserved immunogenic site.
  • Structural modeling revealed that Lys-114 (in a beta E-beta F loop) and Pro-240/Thr-241 (C-terminal region) are spatially close on the assembled capsid due to interactions between adjacent VP1 protomers.

Conclusions:

  • The primary immunogenic site on the ERAV capsid is likely formed by the interaction of residues from different VP1 molecules, specifically Lys-114 from one protomer and Pro-240/Thr-241 from an adjacent protomer.
  • This structural arrangement of the immunogenic site in ERAV is analogous to Immunogenic Site 1 of FMDV, suggesting conserved mechanisms in picornavirus capsid structure and antigenicity.
  • These findings provide critical insights into ERAV's antigenic structure, aiding in the design of more effective vaccines and diagnostic tools.

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