Mapping a Type-specific Epitope by Monoclonal Antibody against VP3 Protein of Duck Hepatitis A Type 1 Virus

Figures

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  Figure 1. VP3 protein detection in pCI-neo-VP3 transfected DEF cells by Western blot. (a) VP3 protein detected with duck anti-DHAV-1 serum. Lane M, protein molecular weight marker. 1, representative pCI-neo-VP3 transfected DEF cells. 2, representative pCI-neo transfected DEF cells. (b) VP3 protein detected with mAbs. 1, representative pCI-neo transfected DEF cells. 2, representative pCI-neo-VP3 transfected DEF cells. Lane M, protein molecular weight marker.

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  Figure 2. VP3 protein detection in DHAV-1/DHAV-3 infected DEF cells by IFA. (A) Representative DHAV-1 infected DEFs detected by mAbs; (B) Representative DHAV-1 infected DEF cells detected with mAbs and then stained with DAPI; (C) Representative DHAV-3-infected DEF/uninfected DEF cells detected by mAbs (negative control).

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  Figure 3. Reactivity of selected phages for mAb 3B7 binding in phage enzyme- linked immunosorbent assay (ELISA). The selected phage clones were detected by mAb 3B7 or the anti‐ porcine interferon (IFN)- c mAb (negative control) after three rounds of iopanning. OD, optical density.

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  Figure 4. Reactivity of synthesized epitope peptides to mAb 3B7 in dot blotting assay. YIRTPACWD and the VP3 protein were used as the negative and positive control, respectively.

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  Figure 5. Sequence alignment of the epitope-coding region in the VP3 protein of duck hepatitis type A strains. Amino acid positions for each sequence are numbered. The sequence for the DHAV-1 HP1 strain is shown at the top; the dashes indicate identical amino acids. The identified epitope region is shadowed in red.

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  Figure 6. The reactivity of the synthesized epitope peptide to duck anti‐ DHAV-1/-DHAV-3 sera by dot blotting. YIRTPACWD and VP3 protein were used as the negative and positive controls, respectively.