Human Anti-RSV F Recombinant Antibody (clone MPE8) (CAT#: PABS-0236)

Figure 1 Antibody ELISA assays with RSV F mutants that disrupt MPE8 binding and lie within the MPE8 epitope (D310A and G307R).

Wen, X., Mousa, J. J., Bates, J. T., Lamb, R. A., Crowe, J. E., & Jardetzky, T. S. (2017). Structural basis for antibody cross-neutralization of respiratory syncytial virus and human metapneumovirus. Nature microbiology, 2(4), 1-7.

Figure 2 ELISA binding curves of the hMPV F protein-specific mAbs.

ELISA binding curves of the isolated mAbs with recombinant hMPV F protein constructs. Prefusion RSV F protein (SC-TM) was utilized to determine if any mAb cross-reacts with RSV F. No cross-reactivity was observed except for mAbs 101F and MPE8. The pneumolysin toxin from Streptococcus pneumoniae was used as a negative binding control. EC50 values are inlaid in each graph and are color-coded according to the key at the top of the curves. Recombinant hMPV F protein constructs are hMPV A1 F (dark blue), hMPV A2 F (light blue), hMPV B1 F (green), hMPV B2 F (red), hMPV B2 F-GCN4 (orange), hMPV A1 F (trypsin) (purple), RSV A2 SC-TM (gray), and Ply (black).

Bar-Peled, Y., Diaz, D., Pena-Briseno, A., Murray, J., Huang, J., Tripp, R. A., & Mousa, J. J. (2019). A potent neutralizing site III-specific human antibody neutralizes human metapneumovirus in vivo. Journal of Virology, 93(19), e00342-19.

Figure 3 Neutralization profiles of the hMPV F protein-specific mAbs.

Shown are neutralization curves for the human mAbs and controls. IC50 values are inlaid on each graph and are color-coded according to the key at the top of each curve.

Bar-Peled, Y., Diaz, D., Pena-Briseno, A., Murray, J., Huang, J., Tripp, R. A., & Mousa, J. J. (2019). A potent neutralizing site III-specific human antibody neutralizes human metapneumovirus in vivo. Journal of Virology, 93(19), e00342-19.

Figure 4 Neutralizing activity of different monoclonal antibodies targeting the RSV F protein of hRSV.

Effective concentrations (EC50) for each ofthe antibodies are indicated above the graphs (in ng/ml). Mota: motavizumab

Steff, A. M., Monroe, J., Friedrich, K., Chandramouli, S., Nguyen, T. L. A., Tian, S., ... & Carfi, A. (2017). Pre-fusion RSV F strongly boosts pre-fusion specific neutralizing responses in cattle pre-exposed to bovine RSV. Nature communications, 8(1), 1-10.

Figure 5 Neutralizing activity of different monoclonal antibodies targeting the RSV F protein of bRSV.

Effective concentrations (EC50) for each ofthe antibodies are indicated above the graphs (in ng/ml). Mota: motavizumab

Steff, A. M., Monroe, J., Friedrich, K., Chandramouli, S., Nguyen, T. L. A., Tian, S., ... & Carfi, A. (2017). Pre-fusion RSV F strongly boosts pre-fusion specific neutralizing responses in cattle pre-exposed to bovine RSV. Nature communications, 8(1), 1-10.

Figure 6 Relative binding of D25, 101F, MPE8 and AM14 to cell surface-expressed prefusion F (grey) or prefusion F containing the AM14 escape mutation, N426D (white) was measured by flow cytometry.

Data were normalized to motavizumab binding. Binding of D25, 101F and MPE8 to N426D was comparable to wild-type prefusion F, whereas AM14 binding to N426D was reduced four-fold (n = 3, P < 0.001; Tukey's HSD, error bars show standard deviation).

Gilman, M. S., Moin, S. M., Mas, V., Chen, M., Patel, N. K., Kramer, K., ... & McLellan, J. S. (2015). Characterization of a prefusion-specific antibody that recognizes a quaternary, cleavage-dependent epitope on the RSV fusion glycoprotein. PLoS pathogens, 11(7), e1005035.

Figure 7 Binding of antibody MPE8.

Binding of antibody MPE8 to uncleaved monomeric RSV F (open black triangles), cleaved monomeric RSV F (black circles), uncleaved postfusion RSV F (open blue triangles), cleaved postfusion RSV F (blue circles), uncleaved prefusion RSV F (open red triangles) and cleaved prefusion RSV F (red circles) was measured by ELISA.

Gilman, M. S., Moin, S. M., Mas, V., Chen, M., Patel, N. K., Kramer, K., ... & McLellan, J. S. (2015). Characterization of a prefusion-specific antibody that recognizes a quaternary, cleavage-dependent epitope on the RSV fusion glycoprotein. PLoS pathogens, 11(7), e1005035.