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Published on: March 24, 2017
A high proportion of anti-peptide antibodies recognize foot-and-mouth disease virus particles
N R Parry1, A Syred, D J Rowlands
1Wellcome Biotech, Beckenham, Kent, U.K.
Abstract:
Synthetic peptides representing the amino acid sequence 141-160 of the structural protein VP1 of foot-and-mouth disease virus (FMDV) elicit virus-neutralizing antibody. Absorption of anti-peptide sera with purified virus particles removed all detectable virus-binding and neutralizing activity, and reduced the ELISA titres against the homologous peptide by 31-41%. The proportion of anti-peptide antibodies that also recognized virus was unaffected by whether the peptide had been inoculated free, carrier-linked or as part of a fusion protein. The majority of these antibodies reacted with sites composed of residues 142-150. Peptides extended at the amino terminus, into regions shown to be poorly antigenic on the intact virus, induced greater neutralizing responses by increasing the proportion of virus-binding antibodies recognizing region 141-150 from 35% to 70%. However, the total proportion of activity against the longer homologous peptide removed by virus absorption remained within the range 31-41%.
Insights
Synthetic peptides targeting foot-and-mouth disease virus (FMDV) VP1 protein can generate neutralizing antibodies. These antibodies primarily recognize specific peptide regions, enhancing FMDV vaccine development potential.
Area of Science:
- Immunology
- Virology
- Molecular Biology
Background:
- Foot-and-mouth disease virus (FMDV) is a significant global livestock pathogen.
- The structural protein VP1 contains epitopes targeted by neutralizing antibodies.
- Understanding peptide-based immunogenicity is crucial for vaccine design.
Purpose of the Study:
- To investigate the immunogenicity of synthetic peptides corresponding to FMDV VP1 amino acid sequence 141-160.
- To characterize the neutralizing antibody response elicited by these peptides.
- To identify the specific regions within the peptide that are recognized by virus-neutralizing antibodies.
Main Methods:
- Synthesis of peptides representing FMDV VP1 (141-160) and extended sequences.
- Immunization of animals with free, carrier-linked, or fusion protein peptides.
- ELISA and virus neutralization assays to quantify antibody responses.
- Antibody absorption experiments using purified FMDV particles.
Main Results:
- Synthetic peptides (141-160) elicited virus-neutralizing antibodies.
- Absorption studies indicated that 31-41% of anti-peptide activity recognized the virus.
- Antibodies predominantly targeted residues 142-150.
- Extended peptides increased virus-binding antibody proportion from 35% to 70% for region 141-150.
Conclusions:
- Synthetic peptides of FMDV VP1 can induce neutralizing antibodies.
- The immunogenicity and neutralizing capacity can be enhanced by extending peptides into poorly antigenic regions.
- These findings support the development of peptide-based vaccines against FMDV.
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