Human Anti-HIV-1 gp120 Recombinant Antibody (clone VRC03) (CAT#: PABL-155)

Figure 1 Analysis of neutralization by MAbs VRC03, VRC06, and VRC06b against a panel of 178 Env pseudoviruses consisting of representatives from the major circulating clades of HIV-1. Dendrograms made by the neighbor-joining method show the protein distances of the Env gp160 sequences derived from 178 HIV-1 isolates. The clade B reference strain HXBc2 was used to root the tree, and the amino acid distance scale is indicated with a value of 1% distance. The clades of HIV-1 group M, including circulating recombinant forms (CRFs), are indicated. Neutralization potency of VRC03, VRC06, and VRC06b is indicated by the color of the branch for each virus. The data under the dendrograms show the percentages of viruses neutralized with an IC50 of <50 μg/ml and <1 μg/ml, and the geometric mean titer (GMT) of IC50 for viruses neutralized with an IC50 of <50 μg/ml.

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M.,... & Chakrabarti, B. (2012). HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully-Cleaved Envelope Glycoproteins. Journal of virology, JVI-01543.

Figure 2 Binding of VRC03, VRC06, and VRC06b to JR-FL gp160ΔCT-transfected 293T cell surface by FACS assay, represented by MFI (mean of fluorescence intensity). JR-FL gp160ΔCT is the cleaved trimer; JR-FL gp160ΔCT cleavage-defective is the uncleaved trimer, which contains two mutations that render it cleavage defective.

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M.,... & Chakrabarti, B. (2012). HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully-Cleaved Envelope Glycoproteins. Journal of virology, JVI-01543.

Figure 3 VRC06 neutralization potency against JR-FL gp160ΔCT virus was affected by Env mutations leading to an alteration of neutralization sensitivity. Top graphs, Env mutants Δ301 and T569A/I675V display enhanced neutralization sensitivity to CD4bs MAb F105 but substantially decreased neutralization sensitivity to VRC06; the bar graphs on the bottom depict the effects of the Env mutations Δ301 and T569A/I675V on the HIV sensitivity (IC50 values) to VRC06 and other CD4bs ligands.

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M.,... & Chakrabarti, B. (2012). HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully-Cleaved Envelope Glycoproteins. Journal of virology, JVI-01543.

Figure 4 VRC06 and VRC06b displayed unique binding properties for Env gp120. (A) VRC06 and VRC06b preferred recognition of Env of CD4-bound conformation (stabilized core, 2CC) and of trimeric context YU2 gp140-F trimer. The CoRbs MAb 17b was used as control.

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M.,... & Chakrabarti, B. (2012). HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully-Cleaved Envelope Glycoproteins. Journal of virology, JVI-01543.

Figure 5 Coexpressed CD4 competes for ligands that recognize the Env CD4-binding site.

Cells expressing HIV-1YU2ΔCT Env together with increasing concentrations of human CD4 were stained by the anti-CD4 OKT4 antibody (A) or the CD4-binding site ligands CD4-Ig, b12, VRC03, and VRC01 (B), using the cell-based ELISA. Data are representative of those obtained in at least three independent experiments performed in triplicate (mean ± SD). Signals were normalized to that obtained with the gp120 outer domain-recognizing antibody 2G12 in the absence of coexpressed CD4.

Veillette, M., Désormeaux, A., Medjahed, H., Gharsallah, N. E., Coutu, M., Baalwa, J.,... & Haynes, B. F. (2014). Interaction with cellular CD4 exposes HIV-1 envelope epitopes targeted by antibody-dependent cell-mediated cytotoxicity.Journal of virology, 88(5), 2633-2644.