Structural analysis of antigenic epitopes was performed using an online computer software program. The spatial conformation of the three epitopes on FAdV-C4 L1-hexon was predicted. Epitopes31PLAPKESMFN40(Fig. 6a, marked with red) and 181DYDDYNIGTT190(Fig. 6a, marked with yellow) are exposed on the surface of the L1-hexon protein, while epitope 79KISGVFPNPNQG90lies within an open-ended groove (Fig. 6a, marked with green). Furthermore, the three mutants of the epitope31PLAPKESMFN40(K35R, S37A, and M38I or M38F) are inserted at the bottom of the protein base (Fig. 6b, marked with blue), while the other amino acid residues are exposed on the surface (Fig. 6b, marked with red). Epitope 31PLAPKESMFN40(5F7) showed the highest antigenic index and hydrophilicity in the analysis of the secondary structure prediction, while epitope79KISGVFPNPNQG90is weak (Fig. 6c).