Cross-Serotype Reactivity of ELISAs Used to Detect Antibodies to the Structural Proteins of Foot-and-Mouth Disease Virus

Antibodies to the foot-and-mouth disease virus (FMDV) capsid induced by infection or vaccination can provide serotype-specific protection and be measured using virus neutralization tests and viral structural-protein (SP-)ELISAs. Separate tests are needed for each serotype, but cross-serotype reactions complicate serotyping. In this study, inter-serotypic responses were quantified for five SP-ELISA formats by testing 294 monovalent mainly bovine sera collected following infection, vaccination, or vaccination and infection with one of five serotypes of FMDV. Over half of the samples, representing all three immunization categories, scored positive for at least one heterologous serotype and some scored positive for all serotypes tested. A comparative approach to identifying the strongest reaction amongst serotypes O, A and Asia 1 improved the accuracy of serotyping to 73–100% depending on the serotype and test system, but this method will be undermined where animals have been infected and/or vaccinated with multiple FMDV serotypes. Preliminary studies with stabilized recombinant capsid antigens of serotypes O and A that do not expose internal epitopes showed reduced cross-reactivity, supporting the hypothesis that capsid integrity can affect the serotype-specificity of the SP-ELISAs. The residual cross-reactivity associated with capsid surface epitopes was consistent with the evidence of cross-serotype virus neutralization.

[1]  Z. Rao,et al.  Structures of Foot-and-mouth Disease Virus with neutralizing antibodies derived from recovered natural host reveal a mechanism for cross-serotype neutralization , 2021, PLoS pathogens.

[2]  Sang Hyun Park,et al.  Development of a Potent Stabilizer for Long-Term Storage of Foot-and-Mouth Disease Vaccine Antigens , 2021, Vaccines.

[3]  K. De Clercq,et al.  The history of foot-and-mouth disease virus serotype C: the first known extinct serotype? , 2021, Virus evolution.

[4]  E. Brocchi,et al.  Development and validation of a simplified serotyping ELISA based on monoclonal antibodies for the diagnosis of foot-and-mouth disease virus serotypes O, A, C and Asia 1. , 2020, Transboundary and emerging diseases.

[5]  G. Belsham.  Towards improvements in foot-and-mouth disease vaccine performance , 2020, Acta Veterinaria Scandinavica.

[6]  M. C. Miraglia,et al.  The role of viral particle integrity in the serological assessment of foot-and-mouth disease virus vaccine-induced immunity in swine , 2020, PloS one.

[7]  S. Berryman,et al.  Detection of Bovine Antibodies against a Conserved Capsid Epitope as the Basis of a Novel Universal Serological Test for Foot-and-Mouth Disease , 2020, Journal of Clinical Microbiology.

[8]  R. Reeve,et al.  Estimating the protection afforded by foot-and-mouth disease vaccines in the laboratory. , 2019, Vaccine.

[9]  S. Cleaveland,et al.  Waves of endemic foot-and-mouth disease in eastern Africa suggest feasibility of proactive vaccination approaches , 2018, Nature Ecology & Evolution.

[10]  S. Berryman,et al.  Truncated Bovine Integrin Alpha-v/Beta-6 as a Universal Capture Ligand for FMD Diagnosis , 2016, PloS one.

[11]  William T. Harvey,et al.  Tracking the Antigenic Evolution of Foot-and-Mouth Disease Virus , 2016, PloS one.

[12]  H. Siegismund,et al.  Challenges for Serology-Based Characterization of Foot-and-Mouth Disease Outbreaks in Endemic Areas; Identification of Two Separate Lineages of Serotype O FMDV in Uganda in 2011. , 2015, Transboundary and emerging diseases.

[13]  D. Stuart,et al.  Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine design , 2015, Nature Structural &Molecular Biology.

[14]  R. Moormann,et al.  Serological evidence indicates that foot-and-mouth disease virus serotype O, C and SAT1 are most dominant in eritrea. , 2014, Transboundary and emerging diseases.

[15]  D. Stuart,et al.  Rational Engineering of Recombinant Picornavirus Capsids to Produce Safe, Protective Vaccine Antigen , 2013, PLoS pathogens.

[16]  K. De Clercq,et al.  Confidence in indirect assessment of foot-and-mouth disease vaccine potency and vaccine matching carried out by liquid phase ELISA and virus neutralization tests. , 2010, Vaccine.

[17]  D. Stuart,et al.  Utility of recombinant integrin αvβ6 as a capture reagent in immunoassays for the diagnosis of foot-and-mouth disease , 2005 .

[18]  T. Doel,et al.  Comparative immunogenicity of 146S, 75S and 12S particles of foot-and-mouth disease virus , 2005, Archives of Virology.

[19]  S. Alexandersen,et al.  Validation of a foot-and-mouth disease antibody screening solid-phase competition ELISA (SPCE). , 2004, Journal of virological methods.

[20]  Bradley P. Carlin,et al.  Bayesian measures of model complexity and fit , 2002 .

[21]  D. Mackay,et al.  A solid-phase competition ELISA for measuring antibody to foot-and-mouth disease virus. , 2001, Journal of virological methods.

[22]  D. Sheppard,et al.  The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virus. , 2000, Journal of virology.

[23]  P. Grigera,et al.  Assessment of foot and mouth disease vaccine potency by liquid-phase blocking ELISA: a proposal for an alternative to the challenge procedure in Argentina. , 1995, Vaccine.

[24]  P. Hingley,et al.  Foot and mouth disease vaccine potency tests in cattle: the interrelationship of antigen dose, serum neutralizing antibody response and protection from challenge. , 1992, Vaccine.

[25]  N. Ferris,et al.  Freeze-drying foot-and-mouth disease virus antigens. II. For use in the ELISA. , 1990, Journal of virological methods.

[26]  N. Ferris,et al.  Freeze-drying foot-and-mouth disease virus antigens. I. Infectivity studies. , 1990, Journal of virological methods.

[27]  R. Meloen,et al.  Evidence for at least four antigenic sites on type O foot-and-mouth disease virus involved in neutralization; identification by single and multiple site monoclonal antibody-resistant mutants. , 1989, The Journal of general virology.

[28]  David Rowlands,et al.  The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution , 1989, Nature.

[29]  R. Kitching,et al.  Enzyme-linked immunosorbent assay (ELISA) for the detection of antibodies against foot-and-mouth disease virus: III. Evaluation of antibodies after infection and vaccination , 1987, Epidemiology and Infection.

[30]  C. Hamblin,et al.  A new enzyme-linked immunosorbent assay (ELISA) for the detection of antibodies against foot-and-mouth disease virus. I. Development and method of ELISA. , 1986, Journal of immunological methods.

[31]  R. Osborne,et al.  Inactivation, purification and stability of 146S antigens of foot and mouth disease virus for use as reagents in the complement fixation test. , 1984, Revue scientifique et technique.

[32]  A. Syred,et al.  Studies on the stability of foot-and-mouth disease virus using absorbance - temperature profiles. , 1983, Developments in biological standardization.

[33]  I. Barnett,et al.  Serological tests for foot and mouth disease in bovine serum samples. Problems of interpretation. , 1982, Revue scientifique et technique.

[34]  R. Meloen,et al.  A study of the cross-reacting antigens on the intact foot-and-mouth disease virus and its 12S Subunits with antisera against the structural proteins. , 1980, The Journal of general virology.

[35]  D. Rowlands,et al.  Evidence for an internal antigen in foot-and-mouth disease virus. , 1969, The Journal of general virology.

[36]  H. O. Calvery.  The laboratory. , 1946, Medical research, a symposium ....