FIG. 2.

(A) SDS-PAGE analysis of purified wild-type β₂ (lane 1), His-tagged TrfA-33 (lane 2), and His-tagged TrfA-33 (ΔLF) (lane 3) proteins. Three to five micrograms of each purified protein was electrophoresed through a 4 to 12% SDS-PAGE gel prior to being stained with Coomassie brilliant blue R-250 (Bio-Rad). Positions of size standards are indicated. (B) Interactions of β₂ with TrfA-33 proteins. Increasing concentrations of β₂ protein were added to TrfA-33 proteins immobilized onto microtiter plates (5 μg/ml, 50 μl/well). Bound β₂ proteins were detected with anti-β₂ antibody. ▪, ΤrfA-33 on plate; ▴, TrfA-33 (ΔLF) on plate; •, binding buffer, no protein on plate. (C) β₂-binding consensus peptide, peptide 14 with the sequence IG QLSLF GV, inhibited the interaction of TrfA-33 and β₂. Microtiter plate assay results showing the inhibition of TrfA-33 and β₂ interaction by addition of various amounts of peptide 14. No inhibition was observed with the control peptide, peptide 4 with the sequence IG QADMA GV. ▪, peptide 14; •, peptide 4.