A monoclonal antibody against the Senecavirus A VP1 protein recognized a conserved, surface-exposed linear epitope identified as 16DTDFSGELA24.
The identification of a conserved, surface-exposed linear epitope in the SVA VP1 protein provides a valuable tool for investigating SVA etiology and protein function.
Senecavirus A (SVA) is a newly emerging picornavirus associated with porcine idiopathic vesicular disease and sudden death in newborn piglets. Currently, no specific vaccines or drugs are available against SVA, highlighting the importance of investigating the immunological characteristics of its key proteins. The VP1 protein of SVA exhibits strong immunogenicity and high sequence conservation, and it is indispensable to the viral life cycle. In the present study, a monoclonal antibody (mAb) against VP1 was generated. A series of truncated VP1 proteins was then expressed to precisely map the epitope recognized by this mAb. The minimal reactive unit was identified as 16DTDFSGELA24. Homology analysis further revealed that this epitope is conserved among different SVA isolates deposited in GenBank. Moreover, AlphaFold prediction, along with PyMOL (Version 3.0.3) and GETAREA analyses, reveals that this epitope resides in the α-helix and loop regions of the three-dimensional structure of the VP1 protein and is surface-exposed. Collectively, these findings indicate that the mAb and its recognized epitope represent valuable tools for investigating SVA etiology and VP1 protein function.
Wu et al. (Tue,) conducted a other in Senecavirus A (SVA) infection. Monoclonal antibody against VP1 protein was evaluated on Identification of the minimal reactive unit (epitope) recognized by the mAb. A monoclonal antibody against the Senecavirus A VP1 protein recognized a conserved, surface-exposed linear epitope identified as 16DTDFSGELA24.