Human Anti-HIV-1 gp120-gp41 Interface Recombinant Antibody (clone CAP248-2B) (CAT#: PABC-425)

Figure 1 Neutralization curves of CAP248-2B against four viral strains (CAP45, CNE52, CAP228, and ZM249) plotted as percentage inhibition (y-axis) versus antibody concentration (x-axis).

Dotted lines indicate y-axis intersections for IC₈₀, IC₅₀, and IC₂₀. The maximum inhibitory percentage achieved against each virus is listed to the right of each curve.

Wibmer, C. K., Gorman, J., Ozorowski, G., Bhiman, J. N., Sheward, D. J., Elliott, D. H., ... & Druz, A. (2017). Structure and recognition of a novel HIV-1 gp120-gp41 interface antibody that caused MPER exposure through viral escape. PLoS pathogens, 13(1), e1006074.

Figure 2 Binding of labelled CAP248-2B to cell-surface anchored HIV-1 Env by flow cytometry, in the presence of increasing concentrations of unlabeled competitor antibody.

Median fluorescence intensity (MFI) is shown on the y-axis, and increasing concentrations of each competitor antibody is plotted on the x-axis. Decreasing MFI signals correspond to increasing competition with CAP248-2B.

Wibmer, C. K., Gorman, J., Ozorowski, G., Bhiman, J. N., Sheward, D. J., Elliott, D. H., ... & Druz, A. (2017). Structure and recognition of a novel HIV-1 gp120-gp41 interface antibody that caused MPER exposure through viral escape. PLoS pathogens, 13(1), e1006074.

Figure 3 ELISA showing binding of CAP248-2B and related mutant antibodies to the BG505(gp120)-CAP45(gp41) chimeric SOSIP trimer.

Absorbance readings are plotted on the y-axis and antibody concentration on the x-axis. CAP256-VRC26.09 and F105 are used are positive and negative control antibodies.

Wibmer, C. K., Gorman, J., Ozorowski, G., Bhiman, J. N., Sheward, D. J., Elliott, D. H., ... & Druz, A. (2017). Structure and recognition of a novel HIV-1 gp120-gp41 interface antibody that caused MPER exposure through viral escape. PLoS pathogens, 13(1), e1006074.