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. 2020 Oct 26;11:5405. doi: 10.1038/s41467-020-19259-x

Fig. 4. Characterization of the BBRF2-BSRF1 heterodimeric interface.

Fig. 4

a SEC analysis of BBRF2Δ-BSRF1Δ interface mutants (Superdex 75). mAU milli-absorption units. The elution peaks are shown as dashed lines of BBRF2Δ-BSRF1Δ heterodimer (orange), BBRF2Δ monomer (green), BSRF1Δ monomer (purple) are overlaid with each sample (red) as references. b The binding affinity of BBRF2Δ (wild-type or mutant) with BSRF1Δ (wild-type or mutant) measured by BLI. BSRF1Δ (wild-type or mutant) at different concentrations was exposed to 10 μg ml−1 His-tagged BBRF2Δ (wild-type or mutant). Source data are provided as a Source Data file. c Schematic showing the designation of the five BSRF1Δ-derived peptides. N denotes the N-loop. d Binding affinity of peptide 1 (P1) and BBRF2Δ measured by BLI. P1 at different concentrations was exposed to 10 μg ml−1 His-tagged BBRF2Δ. Source data are provided as a Source Data file. e P1 competes with BSRF1Δ in binding to BBRF2Δ. 200 nM BBRF2Δ mixed with different concentrations of P1 was exposed to 10 μg ml−1 immobilized BSRF1Δ. Source data are provided as a Source Data file. f TAT-P1 reduces the numbers of EBV genome copies in a concentration-dependent manner. Error bar indicates s.d. (n = 3). Source data are provided as a Source Data file.