Human Anti-HIV-1 gp41 Recombinant Antibody (clone m66) (CAT#: PABL-189)

Figure 1 Residues of the m66.6 CDR L1 were swapped into the CDR L1 of m66 as listed, and the resulting variants tested for HIV-1 neutralization.

Ofek, G., Zirkle, B., Yang, Y., Zhu, Z., McKee, K., Zhang, B.,... & Mascola, J. R. (2014). Structural basis for HIV-1 neutralization by 2F5-like antibodies m66 and m66. 6. Journal of virology, 88(5), 2426-2441.

Figure 2 Role of CDR H3 loop in recognition of MPER in lipid environment and in HIV-1 neutralization.

(A) Binding profiles of antibodies m66.6 (black), 2F5 (brown), and 11F10 (gray) to gp41 MPER, competed with either liposomal (left panel) or soluble (right panel) MPER. Although all three antibodies were competed by the soluble competitor (right panel), only antibodies m66.6 and 2F5 were competed by the liposomal MPER competitor (left panel). (B) Binding profiles of m66.6 CDR H3 hydrophobicity variants to gp41 MPER. The curves represent the percent binding to the respective liposomal (left panel) or soluble (right panel) MPER competitors. Altered hydrophobicity of the m66.6 CDR H3 had a minimal effect on binding to soluble MPER. Mutations that degraded m66 CDR H3 hydrophobicity reduced antibody recognition of liposomal MPER, while those that augmented hydrophobicity enhanced recognition of liposomal MPER. (C) Role of CDR H3 loop hydrophobicity in the context of the less broad antibody m66. Mutation Y100eHCW was introduced into the CDR H3 loop and virus neutralization tested against a 41-isolate panel. The breadth-potency curve of m66-Y100eHCW (black) is shown in comparison to that of WT m66 (blue).

Ofek, G., Zirkle, B., Yang, Y., Zhu, Z., McKee, K., Zhang, B.,... & Mascola, J. R. (2014). Structural basis for HIV-1 neutralization by 2F5-like antibodies m66 and m66. 6. Journal of virology, 88(5), 2426-2441.