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Generation of a subtype-specific neutralization epitope in foot-and-mouth disease virus of a different subtype
J Hernández1, M A Martínez, E Rocha
1Centro de Biología Molecular, Universidad Autónoma de Madrid, Spain.
Abstract:
An epitope involved in neutralization of foot-and-mouth disease virus (FMDV) of subtype C3 was generated by a single amino acid replacement in VP1 of FMDV of subtype C1. The replacement [Ser (139)----Ile, in the immunodominant site A] was consistently found in those FMDV C1 Santa Pau-Sp/70 mutants resistant to neutralization by monoclonal antibody (MAb) SD6 (specific for most C1 viruses) that acquired the capacity to be neutralized by MAb 7AB5 (specific for C3 viruses).
Insights
A single amino acid change in foot-and-mouth disease virus (FMDV) VP1 protein created a new neutralization epitope. This mutation allowed FMDV C1 viruses to evade one antibody and become susceptible to another, altering viral subtype specificity.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Foot-and-mouth disease virus (FMDV) poses a significant threat to livestock globally.
- Viral neutralization is a key mechanism for controlling FMDV spread.
- Specific epitopes on viral proteins, like VP1, are critical targets for neutralizing antibodies.
Purpose of the Study:
- To investigate the generation of a novel neutralization epitope in FMDV.
- To understand the role of specific amino acid substitutions in altering FMDV neutralization.
- To analyze the impact of mutations on FMDV subtype specificity and antibody interactions.
Main Methods:
- Site-directed mutagenesis was employed to introduce a single amino acid replacement (Ser139Ile) in the VP1 protein of FMDV subtype C1.
- Neutralization assays were performed using specific monoclonal antibodies (MAbs) targeting different FMDV subtypes (MAb SD6 for C1, MAb 7AB5 for C3).
- Analysis of FMDV mutants resistant to MAb SD6 and susceptible to MAb 7AB5.
Main Results:
- A single amino acid replacement (Ser139Ile) in VP1 of FMDV C1 generated an epitope involved in FMDV C3 neutralization.
- Mutants with this replacement became resistant to neutralization by MAb SD6 (specific for C1 viruses).
- These mutants simultaneously acquired the capacity to be neutralized by MAb 7AB5 (specific for C3 viruses).
Conclusions:
- A single amino acid substitution in FMDV VP1 can significantly alter its antigenic properties and neutralization profile.
- This study demonstrates the potential for generating novel epitopes through targeted mutations, impacting viral subtype specificity.
- Understanding these molecular mechanisms is crucial for developing effective FMDV vaccines and diagnostic tools.