Fig. 2
The C-terminal domain of A20 (A20 C-ter) interacts with VACV E9. a Elution profiles from SEC are compared. A20 C-ter and E9 were either loaded separately or mixed together prior to injection onto the column. b SDS-PAGE analysis of the eluted fractions for each run. c Alignment of the last amino acids of A20 using representative viruses from each genus of the Chordopoxvirinae subfamily: VACV, CPXV (cowpox virus), MPXV (monkeypox virus), CMLV (camelpox virus), ECTV (ectromelia virus), VARV (variola virus), YKPV (yokapox virus), LSDV (lumpy skin disease virus), TANV (tanapox virus), SWPV (swinepox virus), MYXV (myxoma virus), MOCV (molluscum contagiosum virus), DPV (deerpox virus), ORFV (ORF virus), CNPV (canarypox virus). Conserved residues are in red. The predicted secondary structure using MLRC66 and its reliability on a 0–9 scale are shown at the bottom of the alignment (ACC). d Helical wheel projection with residues of A20 predicted to fold as an α-helix (aa 400–417). Hydrophilic residues are presented as circles, hydrophobic residues as diamonds, charged residues as triangles and pentagons. e A point mutation in A20 C-ter abrogates binding to E9. A20 C-ter-Phe414Ala was incubated with WT E9 before injection onto SEC. The eluted fractions were analyzed as in b
