Biosensor characterization of antigenic site A of foot-and-mouth disease virus presented in different vector systems

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.

A Fluorescence Resonance Energy Transfer Sensor Based on Maltose Binding Protein

“…Potential applications of these sensor complexes include direct use of their maltose sensing capabilities in food production and processing (16), specifically in beer and bread production which utilize maltose as the primary sugar source and potentially other fermentative technology. Additionally, variants of this sensing scheme may be adapted for glucose monitoring of diabetic patients (8,25) or for sensing of surface glycoproteins of potential antigens (27).…”

A Brief Review on Diagnosis of Foot-and-Mouth Disease of Livestock: Conventional to Molecular Tools

“…In the serological diagnosis of infectious diseases, the use of allosteric biosensors, namely, hybrid enzymes that respond enzymatically to antibodies directed to foreign peptides displayed on the enzyme surface [216,217], is highly promising [218]. Multiple insertions of a major FMDV Bcell epitope from the VP1 capsid protein near the active site of recombinant β-galactosidases dramatically increased the enzyme responsiveness to specific antipeptide antibodies, including sera from infected animals [219,220]. It has been reported that recombinant β-galactosidases accommodating one or two different peptides from the FMDV NS protein 3B per enzyme monomer can be reactivated by anti-3B monoclonal antibodies (MAbs) and these recombinant βgalactosidases could be also efficiently reactivated by sera from infected animals that permitted differentiation between sera from infected animals and those from naïve and conventionally vaccinated pigs.…”