ArticleScientific reports2019
Construction, Expression and Evaluation of Recombinant VP2 Protein for serotype-independent Detection of FMDV Seropositive Animals in Egypt.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Development of a Competitive Chemiluminescent Enzyme Immunoassay Based on Recombinant FMDV VP2 Protein for Rapid and Simultaneous Detection of Antibodies Against Foot-and-Mouth Disease Virus Serotypes O and A.Veterinary sciences · 2026Article
- Ribosomal protein L35 negatively regulates FMDV replication by recruiting AMFR to promote the ubiquitination and degradation of VP2.Journal of virology · 2025Article
- N-terminal truncation of the foot-and-mouth disease virus VP0 protein promotes soluble co-expression and particle assembly stability of viral capsid proteins in Escherichia coli.BMC biotechnology · 2025Article
- Design and application of expression constructs for FMDV serotype O structural proteins.Biotechnology letters · 2025Article
- Epidemiological and Genetic Insights of the Circulating Foot-and-Mouth Disease Virus Serotypes in Egypt.Current microbiology · 2024Article
- A comprehensive and single-use foot-and-mouth disease sero-surveillance prototype employing rationally designed multiple viral antigens.Scientific reports · 2024Article
- Circulating foot-and-mouth disease virus serotype A African-genotype IV in Egypt during 2022.Veterinary world · 2023Article
- A gold nanoparticles-based lateral flow assay utilizing baculovirus expressed recombinant nucleocapsid and receptor binding domain proteins for serodetection of IgG and IgM against SARS-CoV-2.Biotechnology letters · 2022Article
- The Use of Distinctive Monoclonal Antibodies in FMD VLP- and P1-Based Blocking ELISA for the Seromonitoring of Vaccinated Swine.International journal of molecular sciences · 2022Article
- Generation and utility of a single-chain fragment variable monoclonal antibody platform against a baculovirus expressed recombinant receptor binding domain of SARS-CoV-2 spike protein.Molecular immunology · 2022Article
- Removal of 3C protease from the 3ABC improves expression, solubility, and purification of the recombinant 3AB of foot-and-mouth disease virus.Virus genes · 2021Article
- Utilization of a recombinant defensin from Maize (Zea mays L.) as a potential antimicrobial peptide.AMB Express · 2020Article
- Characterization, cloning, expression and bioassay ofSaudi journal of biological sciences · 2020Article
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Authors and funding
6 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Foot-and-mouth disease virus (FMDV) is one of the most devastating viral pathogens of cloven-hoofed animals. The detection of antibodies (Ab) against FMDV structural proteins (SP) using virus neutralization test (VNT) and liquid-phase blocking ELISA (LPBE) is the standard procedure in use for monitoring seroconversion in animals post vaccination, the prevalence of infection-surveillance, proving clinical cases and seronegative status of FMDV-free/naïve-animals prior transportation. However, due to variations within SP of FMDV serotypes, each serotype-specific Ab should be detected separately which is laborious and time-consuming. Accordingly, it is crucial to develop a sensitive, rapid, and accurate test capable of detecting FMDV-specific Ab, regardless its serotype. This study describes the heterologous expression of VP2 protein in E. coli, and its evaluation as a capture antigen in a simple indirect ELISA for serotype-independent detection of anti-FMDV Ab. Sequence analysis revealed that the VP2-coding sequence is considerably conserved among FMDV serotypes. The recombinant VP2 (rVP2), a 22 kDa polypeptide, was purified to near homogeneity by affinity chromatography under native conditions. Immunoreactivity of the rVP2 was confirmed by using a panel of positive sera including sera from animals vaccinated with the local trivalent vaccine and guinea pig FMDV antiserum, which is routinely used as tracing/detecting Ab in LPBE testing. The results obtained from the VP2-based ELISA were comparable to those determined by VNT and LPBE standard diagnostic assays. Specificity and sensitivity of rVP2 in capturing anti-FMDV Ab were 98.3% and 100%, respectively. The developed VP2-ELISA is proved reliable and time-efficient assay for detection of FMDV seropositive animals, regardless the FMDV serotype that can be implemented in a combination with VNT and/or LPBE for rapid diagnosis of an ongoing FMDV infection.
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