Human Anti-HIV-1 gp120 Recombinant Antibody (clone MAb 2158) (CAT#: HPAB-S0052-YC)

Figure 1 Representative neutralization curves for MAbs against SF162 and JR-FL parental and JR(SF-V1/V2) and SF(JR-V1/V2) Env pseudotypes.

The preferential neutralization of the SF162 Env seen with most of the MAbs tested also correlated with the origin of the V1/V2 domain.

Pinter, A., Honnen, W. J., He, Y., Gorny, M. K., Zolla-Pazner, S., & Kayman, S. C. (2004). The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection. Journal of virology, 78(10), 5205-5215.

Figure 2 MAb 2158 binding of V2 mutants.

Point mutations were introduced into the 1FD6 scaffolded V1V2 (CAP45 sequence) and tested for binding with MAb 2158. Mutants were made to interrogate positions in the strand B-C region (residues 160 to 171) (A), the strand C tail region (residues 172 to 175) (B), the integrin binding site (residues 179 to 181) (C), and the variable sequence region (residues 183 to 193) (D). The ELISA result for each mutation is shown as a percentage of binding relative to that of the wild type (WT).

Spurrier, B., Sampson, J., Gorny, M. K., Zolla-Pazner, S., & Kong, X. P. (2014). Functional implications of the binding mode of a human conformation-dependent V2 monoclonal antibody against HIV. Journal of virology, 88(8), 4100-4112.