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Antigenic comparison of different foot-and-mouth disease virus types using monoclonal antibodies defining multiple
J C Saiz1, M J Gonzalez, D O Morgan
1Molecular Biology Laboratory, USDA-Agricultural Research Service, Greenport, NY 11944.
Abstract:
Thirteen monoclonal antibodies (MAbs) were elicited with A5 Spain-86 virus, the cause of the most recent foot-and-mouth disease virus (FMDV) outbreak in Spain. The MAbs were tested for ability to bind 140S virions and 12S protein subunits by liquid-phase radioimmunoassay (RIA), and to bind VP1 capsid protein by Western immunoblot assay. One of the thirteen MAb was virion (140S) specific, seven recognized 140S and 12S subunits, one bound to 140S, 12S and VP1 and four were 12S specific. These MAbs presented varying binding patterns when tested against different FMDV subtypes and serotypes, indicating the presence of conserved and non-conserved epitopes among FMDV serotypes and subtypes. Neutralization assays, in vivo and in vitro, showed that none of the 140S specific MAbs or 12S specific MAbs were neutralizing, but notably several of the 12S specific MAbs bound to all the different FMDV serotypes and can be useful diagnostic reagent for the detection of FMDV. The remaining MAbs showed varying behavior with the different types tested: not all types to which the MAbs bound were neutralized, demonstrating that the presence of an epitope and subsequent neutralization of infectivity are not necessarily correlated. Five type A12 neutralizing MAbs, previously characterized, have been used in this work. Four bound to A5 Spain-86 virus, but only one neutralized viral infectivity. On the basis of differential reactivity and neutralization among various FMDV subtypes and serotypes, and cross-inhibition binding assays between these MAbs, seven neutralization related epitopes have been defined on A5 Spain-86 virus.
Insights
Thirteen monoclonal antibodies (MAbs) targeting foot-and-mouth disease virus (FMDV) were developed. Some MAbs show broad FMDV serotype binding for diagnostics, though neutralization varied, revealing complex epitope-neutralization relationships.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Foot-and-mouth disease virus (FMDV) poses a significant threat to livestock globally.
- Understanding FMDV epitopes is crucial for developing effective vaccines and diagnostics.
- Previous studies have characterized some neutralizing antibodies against FMDV.
Purpose of the Study:
- To characterize monoclonal antibodies (MAbs) elicited against the A5 Spain-86 FMDV strain.
- To investigate the binding specificities of these MAbs to different FMDV components and serotypes.
- To assess the neutralizing capacity of MAbs and define neutralization-related epitopes.
Main Methods:
- Production and characterization of thirteen MAbs against A5 Spain-86 FMDV.
- Liquid-phase radioimmunoassay (RIA) to test binding to 140S virions and 12S protein subunits.
- Western immunoblot assay to assess binding to VP1 capsid protein.
- In vivo and in vitro neutralization assays.
- Cross-inhibition binding assays.
Main Results:
- One MAb was 140S specific, seven recognized 140S and 12S subunits, one bound to 140S, 12S, and VP1, and four were 12S specific.
- MAbs exhibited varying binding patterns across different FMDV serotypes and subtypes, indicating conserved and non-conserved epitopes.
- Several 12S-specific MAbs showed broad reactivity against all tested FMDV serotypes, suggesting potential as diagnostic reagents.
- None of the 140S or 12S specific MAbs were neutralizing.
- Only one of four previously characterized neutralizing MAbs bound to and neutralized the A5 Spain-86 virus.
- Seven neutralization-related epitopes were defined on the A5 Spain-86 virus.
Conclusions:
- Monoclonal antibodies against FMDV can have diverse binding specificities and neutralizing activities.
- Some FMDV epitopes are conserved across serotypes, making MAbs targeting them useful for diagnostics.
- Antibody binding to viral components does not always correlate with infectivity neutralization.
- Defining neutralization-related epitopes is essential for understanding FMDV immunopathogenesis and vaccine design.