Human Anti-HIV-1 Env Recombinant Antibody (clone VRC03b) (CAT#: MRO-2804CQ)

Figure 1 Comparison of reactivities of selected HIV-1 gp120-specific monoclonal antibodies with native and deglycosylated recombinant HIV-1 gp120 analyzed by ELISA.

ELISA plates were coated with anti-penta-His antibody followed by capture of equal amounts of gp120 produced in HEK 293T (abbreviated as 293), Jurkat, RD, HepG2, or CHO cells (0.05 μg gp120 per well). gp120 preparations were in native form (black columns) or deglycosylated with PNGase F (grey columns). Monoclonal antibody VRC03 was added and the bound IgG antibodies were detected with HRP-conjugated goat anti-human IgG.

Raska, M., Czernekova, L., Moldoveanu, Z., Zachova, K., Elliott, M. C., Novak, Z., ... & Smith, P. D. (2014). Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection. AIDS research and therapy, 11(1), 23.

Figure 2 Binding of VRC03, VRC06, and VRC06b to JR-FL gp160 CTtransfected 293T cell surface by FACS assay, represented by MFI (mean of fluorescence intensity).

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M., ... & Chakrabarti, B. K. (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, 86(20), 11231-11241.

Figure 3 VRC03 and related MAbs recognized quaternary epitopes on Env functional trimer.

VRC06 neutralization potency against JR-FL gp160 CT virus was affected by Env mutations leading to an alteration of neutralization sensitivity.The graph depicts the effects of the Env mutations 301 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. K. (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, 86(20), 11231-11241.

Figure 4 VRC06 and VRC06b displayed unique binding properties for Env gp120.

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. K. (2012). HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelopglycoproteins. Journal of virology, 86(20), 11231-11241.

Figure 5 FACS-based binding curves of MAbs to the cell surface JRFL-cleaved trimers.

The CD4bs-directed bNabs

Chakrabarti, B. K., Feng, Y., Sharma, S. K., McKee, K., Hedestam, G. B. K., LaBranche, C. C., ... & Wyatt, R. T. (2013). Robust neutralizing antibodies elicited by HIV-1 JRFL envelope glycoprotein trimers in nonhuman primates. Journal of virology, 87(24), 13239-13251.

Figure 6 Binding kinetics of selected Fabs and IgGs to the JRFL gp140-F trimers.

Assessed binding of the full IgGs for PGV04 and VRC03 compared to 17b as assessed by Octet bio-layer interferometry.

Chakrabarti, B. K., Feng, Y., Sharma, S. K., McKee, K., Hedestam, G. B. K., LaBranche, C. C., ... & Wyatt, R. T. (2013). Robust neutralizing antibodies elicited by HIV-1 JRFL envelope glycoprotein trimers in nonhuman primates. Journal of virology, 87(24), 13239-13251.