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Two mechanisms of antigenic diversification of foot-and-mouth disease virus

M A Martínez1, J Hernández, M E Piccone

  • 1Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma de Madrid, Spain.

Virology
|October 1, 1991
PubMed

Insights

Foot-and-mouth disease virus (FMDV) antigenic variation is driven by amino acid changes in VP1 protein. These changes, particularly at site A, cause gradual or abrupt shifts in viral epitopes, impacting vaccine design.

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Foot-and-mouth disease virus (FMDV) poses a significant threat to livestock globally.
  • Antigenic variation in FMDV, particularly within serotype C, complicates vaccine efficacy.
  • Understanding the molecular basis of antigenic drift is crucial for developing effective control strategies.

Purpose of the Study:

  • To identify amino acid replacements responsible for antigenic diversification in FMDV serotype C, focusing on antigenic site A.
  • To correlate capsid protein VP1 sequence variations with changes in viral antigenicity.
  • To elucidate the mechanisms driving antigenic change in FMDV.

Main Methods:

  • Sequencing of 16 VP1 genes from FMDV serotype C isolates spanning 1926-1989.
  • Enzyme-linked immunoelectrotransfer blot (EITB) assays using neutralizing monoclonal antibodies against antigenic sites A and C.
  • Correlation of VP1 amino acid sequences with antibody reactivity to map antigenic epitopes.

Main Results:

  • Identified amino acid substitutions within VP1 residues 138-150 (site A) that underlie FMDV antigenic variation.
  • Revealed two mechanisms of antigenic change: gradual antigenic distance increase via accumulated replacements and abrupt change due to critical single-residue substitutions.
  • Demonstrated that specific replacements, such as Ala(145) to Val or His(146) to Gln, can cause significant epitope loss.

Conclusions:

  • The study provides detailed insights into the molecular mechanisms of FMDV antigenic variation within serotype C.
  • Identified key amino acid substitutions offer valuable information for the rational design of synthetic FMDV vaccines.
  • Despite extensive variation observed over six decades, FMDV appears to retain significant potential for further antigenic evolution within serotype C.

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