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. 2014 Aug 19;211(3):462–471. doi: 10.1093/infdis/jiu460

Figure 1.

Figure 1.

A, B, BB0238 interacts with BB0323. Far-Western blot analyses demonstrate specific binding of BB0238 to BB0323 (A) or binding of BB0323 to BB0238 (B). The recombinant proteins (either BB0238 or BB0323) were separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and incubated with glutathione S-transferase (GST)–fused proteins (either BB0323 or BB0238) or GST (control). Bound proteins were detected by anti-GST antibodies conjugated to horseradish peroxidase. Arrows denote the position of the band specifically detected by the recombinant protein; asterisk, either a nonspecific band or a degraded form of BB0323. Migration of protein standards is shown to the left in kilodaltons. C, Schematic representation of various truncated recombinant BB0323 proteins representing N- and C-terminal polypeptides. Truncated polypeptides were produced with or without GST tags. D, BB0238 binds to the N-terminal BB0323. Left panel denotes far-Western analysis; recombinant BB0238 proteins were separated by SDS-PAGE, blotted onto nitrocellulose membranes, and incubated with GST-fused N1 (GST-N1), GST-fused N3 (GST-N3), GST, or GST-fused C-terminal polypeptide (GST-C). Bound proteins were detected with immunoblotting using anti-GST antibodies. Only N-terminal polypeptides exhibit detectable interaction in the assay. Equal protein loading is indicated by immunoblotting using BB0238 antibody (right panel).