Identification of a Common Conformational Epitope on the Glycoprotein E2 of Classical Swine Fever Virus and Border Disease Virus

Figures

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  Figure 1. Inhibition of CSFV binding to PK15 cells by recombinant expressed full-length or partial E2 proteins. For this purpose, the full-length E2 protein and domain B/C (E2_B/C) were used. The numbers within the names of the E2 constructs refer to the protein amounts (µg) per 24-well. The data represent the mean and standard deviation of three independent experiments. Values with different superscript letters, a–c, indicate a statistically significant difference (p < 0.05) from each other. The superscript letter “a” indicates the highest reduction of binding and “c” indicates unchanged binding to cells No significant differences exist between values containing the same letter.

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  Figure 2. Inhibition of CSFV binding to porcine cells by three mAbs specific for glycoprotein E2 and polyclonal CSFV antiserum. An equal amount of each mAb was used (10 µg). The data represent the mean and standard deviation of three independent experiments. Values with different superscript letters, a–c, indicate a statistically significant difference (p < 0.05) from each other. The superscript letter “a” indicates the highest and “c” indicates the lowest reduction of binding to cells among the compared groups. No significant differences exist between values containing the same letter.

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  Figure 3. Alignment of the amino acid sequences of residues 690–738 of pestivirus glycoprotein E2. The positions of amino acid residues are numbered based on those of CSFV strain TD/96/TWN. Sequences are clustered based on their allocation to genotypes as in Table 1. For each virus strain the genotype and the accession number are indicated. The key residues which might be responsible for the reactivity patterns of the mAbs characterized in this study are boxed and highlighted with different colors. The residues P709, L709, E713, G725, V738 and I738 are highlighted with light blue, pink, blue, green, orange and red, respectively. Cysteine residues are indicated by an asterisk above the alignment.

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  Figure 4. The 3D structure modeling of E2 of CSFV strain TD/96. The domain B/C is colored yellow. The residues P709, E713, G725 and I738 recognized by mAbs are highlighted with dark blue, light blue, light green and red, respectively. The mAbs recognizing the highlighted amino acid residues are indicated in boxes.