Key result
The motif (6)ETTLLE(11) of the FMDV VP2 protein is the minimal requirement of the epitope recognized by the serotype-independent monoclonal antibody 4B2.
The fine mapping of the FMDV VP2 epitope recognized by MAb 4B2 suggests its potential utility in FMDV diagnosis.
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May support serotype-independent FMDV diagnostics; leaves open validation in field and clinical settings.
VP2 is a structural protein of the foot-and-mouth disease virus (FMDV). In this study, a FMDV serotype-in-dependent monoclonal antibody (MAb), 4B2, was generated. By screening a phage-displayed random 12-peptide library, we found positive phages displaying the consensus motif ETTXLE (X is any amino acid (aa)), which is highly homologous to (6)ETTLLE(11) at the N-terminus of the VP2 protein. Subsequently, a series of GST-fusion proteins expressing a truncated N-terminus of VP2 were examined by western blot analysis using the MAb 4B2. The results indicated that the motif (6)ETTLLE(11) of VP2 may be the minimal requirement of the epitope recognized by 4B2. Moreover, a 12-aa peptide (2)KKTEETTLLEDR(13) was shown to be the minimal unit of the epitope with maximal binding activity to 4B2. Alanine-scanning analysis demonstrated thatThr(7), Thr(8), and Leu(10) are the functional residues of the 4B2 epitope Glu(6) and Leu(9) are required residues, and Glu(11) plays a crucial role in the binding of MAb 4B2. The fine mapping of the epitope indicated that MAb 4B2 has the potential to be used in FMDV diagnosis.
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Yu et al. (2011) studied Foot-and-mouth disease virus (FMDV). Monoclonal antibody 4B2 was evaluated on Epitope mapping of VP2 protein recognized by MAb 4B2. The motif (6)ETTLLE(11) of the FMDV VP2 protein is the minimal requirement of the epitope recognized by the serotype-independent monoclonal antibody 4B2.
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