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Biosensor characterization of antigenic site A of foot-and-mouth disease virus presented in different vector systems
A Benito1, M H Van Regenmortel
1Immunochemistry Laboratory (UPR9021), Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France.
Abstract:
The region 141-160 of the VP1 protein of foot-and-mouth disease virus known as site A is an immunodominant region that has been extensively studied for the purpose of developing a synthetic vaccine. In the present study, site A of foot-and-mouth disease virus was inserted in three different loops of the maltose-binding protein and its antigenicity was compared with site A presented as a conjugated synthetic peptide or inserted in beta-galactosidase. The affinity of antibodies elicited against the site A synthetic peptide was also compared with that of antibodies raised against the site A inserted within the two carrier proteins. Using biosensor technology it was possible to estimate the concentration of site A antibodies present in the various antisera and to show that site A fused to maltose-binding protein was a slightly better mimic of the epitope present in the virus particle than the synthetic peptide or the beta-galactosidase recombinant construct.
Insights
Site A from foot-and-mouth disease virus (FMDV) was inserted into carrier proteins to mimic the viral epitope. Maltose-binding protein fusion better mimicked the FMDV site A epitope compared to other constructs.
Area of Science:
- Virology
- Immunology
- Biotechnology
Background:
- Site A (residues 141-160) of the foot-and-mouth disease virus (FMDV) VP1 protein is an immunodominant region.
- Extensive research targets Site A for synthetic vaccine development.
Purpose of the Study:
- To compare the antigenicity of Site A when presented in different formats: fused to maltose-binding protein (MBP), conjugated as a synthetic peptide, or inserted into beta-galactosidase (β-gal).
- To evaluate the antibody affinity elicited by these different presentations.
Main Methods:
- Site A was genetically inserted into three loops of MBP.
- Antigenicity and antibody affinity were assessed using biosensor technology.
- Antibodies were raised against Site A synthetic peptide and Site A-fused carrier proteins.
Main Results:
- Site A fused to MBP demonstrated superior mimicry of the FMDV epitope compared to Site A-conjugated peptide or Site A-inserted β-gal.
- Biosensor technology enabled quantification of Site A antibodies in antisera.
- Antibody affinity varied depending on the carrier protein used.
Conclusions:
- Fusion of FMDV Site A to MBP offers a promising strategy for developing subunit vaccines.
- MBP serves as an effective carrier protein for presenting viral epitopes.
- Further studies can explore MBP-based constructs for FMDV vaccine development.
