Anti-S. Aureus Recombinant Antibody (Tefibazumab) (CAT#: TAB-029)

Figure 1 SPR analysis of the ligand interactions and inhibitions.

(A) Two-fold serial dilution of ClfA 229–545 (from 32 to 1 nM) were injected to a tefibazumab surface (~150 RU captured by goat anti-human IgG (Fc) polyclonal F(ab') 2 ). SPR sensorgrams shown in black were fitted to a 1:1 Langmuir binding model curves shown in red. The derived dissociation constant K D (0.81 nM) was calculated from the rate constants (k a = 5.94 × 10 5 M −1 s −1 and k d = 4.90 × 10 −4 s −1 ). (B) ClfA 229–545 (from 1.28 to 0.04 μM) was injected to a Fg surface (10,000 RU on CM5 chip). The average responses at steady state (shown in red) were plotted as a function of the ClfA 229–545 concentration and fit to a one-site binding (hyperbola) model (inset). K D of 0.66 μM was determined.

Ganesh, V. K., Liang, X., Geoghegan, J. A., Cohen, A. L. V., Venugopalan, N., Foster, T. J., & Hook, M. (2016). Lessons from the crystal structure of the S. aureus surface protein clumping factor A in complex with Tefibazumab, an inhibiting monoclonal antibody. EBioMedicine, 13, 328-338.

Figure 2 SPR analysis of the ligand interactions and inhibitions.

Dose response for the inhibition of different concentrations (from 0.125 to 4 μM) of tefibazumab (C) or Fg (D) on 1 μM of ClfA 229–545 binding to immobilized Fg. The maximum 100% response is ClfA 229–545 binding without any inhibitors and shown as dashed lines. (E) Inhibition data from C&D were plotted against inhibitor concentrations (the monomer Fg concentration was used) and fitted to a four-parameter logistic function. The control is for the binding response without any inhibitor. The tefibazumab IC 50 measured for inhibiting ClfA 229–545 binding to Fg is 0.39 μM and the fitted minimum is 27%, the Fg IC 50 is 0.48 μM and the fitted minimum is 0%. The binding of the inhibitors (at the highest concentration of 4 μM) to the Fg surface were very small (b10 RU), compared to the ClfA response of ~ 550 RU, so they were not subtracted from the total responses. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Ganesh, V. K., Liang, X., Geoghegan, J. A., Cohen, A. L. V., Venugopalan, N., Foster, T. J., & Hook, M. (2016). Lessons from the crystal structure of the S. aureus surface protein clumping factor A in complex with Tefibazumab, an inhibiting monoclonal antibody. EBioMedicine, 13, 328-338.

Figure 1 Anti-S. Aureus Recombinant Antibody (TAB-029) in SDS-PAGE

SDS-PAGE analysis of TAB-029 in non-reduced (Lane 1) and reduced (Lane 2) conditions.

Figure 2 Anti-S. Aureus Recombinant Antibody (TAB-029) in HPLC

HPLC analysis of TAB-029 shows the purity is>95%.