This recombinant monoclonal antibody to RSV F and HMPV F is a Human monoclonal antibody that can be used for applications: BLI, Neut, Block, ELISA. This antibody was isolated from human B cells based on its ability to cross-neutralize a panel of RSV and HMPV strains.
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.
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
See more details about Hi-Affi™ recombinant antibody benefits.
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CAT | Product Name | Application | Type |
---|---|---|---|
TAB-009 | Anti-RSV Recombinant Antibody (Palivizumab) | IF, IP, Neut, FuncS, ELISA, FC, WB | IgG1 - kappa |
TAB-709 | Anti-RSV glycoprotein F Recombinant Antibody (Motavizumab) | IF, IP, Neut, FuncS, ELISA, FC, WB | IgG1 - kappa |
MRO-1209LC | Anti-HRSV F Recombinant Antibody (MEDI-493) | ELISA, Neut, PK | Humanized antibody |
MRO-1209LC-S(P) | Anti-HRSV F Recombinant Antibody scFv Fragment (MEDI-493) | ELISA | Humanized antibody |
MRO-1209LC-F(E) | Anti-HRSV F Recombinant Antibody Fab Fragment (MEDI-493) | ELISA | Humanized antibody |
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(Creative Biolabs Cat# PABS-0236, RRID: AB_3111680)
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For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.
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