Key result
A panel of 25 monoclonal antibodies against the VP1 protein of porcinophilic foot-and-mouth disease virus was produced and characterized for neutralization and epitope recognition.
The study successfully produced and characterized a panel of monoclonal antibodies against the porcinophilic FMDV VP1 protein, which may be useful for future vaccine and diagnostic research.
Monoclonal antibodies (MAbs) reported here were produced against the porcinophilic foot-and-mouth disease virus (FMDV) that caused the devastating swine disease on 1997 in Taiwan. A panel (25) of MAbs were found to react with VP1 of O/Taiwan/97 (O/97) by ELISA with various potencies. The biological identities of these VP1 reacting MAbs, such as neutralization activity, isotype and capability to distinguish between two serotype O FMDVs, O/97 and O/Taiwan/KM1/99 (O/99), were further analyzed. Eleven out of the total eighteen O/97 neutralizing MAbs were able to neutralize heterologous O/99. Eight O/97 neutralizing and five non-neutralizing MAbs could differentiate two serotype O FMDVs by immunofluorescence assay (IFA) implied that these thirteen MAbs recognized O/97 specific epitope(s). Furthermore, reactivities of the VP1 reacting MAbs with a 29 amino acids synthetic peptide (P29) representing the betaG-betaH loop of VP1 were analyzed by ELISA and fourteen were found positive. MAb clone Q10E-3 reacting strongest with VP1 and P29, neutralizing both but not differentiating two serotype O viruses suggested that the antibody binding site might involve the RGD motif and its C terminal conserved region on betaG-betaH loop. MAbs with diverse characters presented in this study were the first raised against porcinophilic FMDV. The complete set of MAbs may be used for further studies of vaccine, diagnostic methods, prophylaxis, etiological and immunological researches on FMDV.
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Cheng et al. (2006) studied Foot-and-mouth disease virus (FMDV). Monoclonal antibodies against VP1 of FMDV was evaluated on MAb characterization (neutralization, IFA, ELISA). A panel of 25 monoclonal antibodies against the VP1 protein of porcinophilic foot-and-mouth disease virus was produced and characterized for neutralization and epitope recognition.
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