Human Anti-HIV-1 Env Recombinant Antibody (clone M4008_N1) (CAT#: PABS-0184)

Figure 1 Neutralization Assessment

Neutralization was performed in duplicate wells, and the data shown are means with SEM.

Jia, M., Liberatore, R. A., Guo, Y., Chan, K. W., Pan, R., Lu, H., ... & Wu, X. (2020). VSV-displayed HIV-1 envelope identifies broadly neutralizing antibodies class-switched to IgG and IgA. Cell host & microbe, 27(6), 963-975.

Figure 2 Epitope Mapping of HIV-1 bNAb

Epitope mapping of bNAbs by comparison of neutralization profiles of each bNAb on the HIV-1 strain JR-FL, as WT, treated with Kifunensine (Kif), or with indicated point mutations. Neutralization was performed in duplicate wells, and the data shown are means with SEM.

Jia, M., Liberatore, R. A., Guo, Y., Chan, K. W., Pan, R., Lu, H., ... & Wu, X. (2020). VSV-displayed HIV-1 envelope identifies broadly neutralizing antibodies class-switched to IgG and IgA. Cell host & microbe, 27(6), 963-975.

Figure 3 Epitope Mapping of HIV-1 bNAb

Epitope mapping of bNAbs by standard and competition ELISAs. The competition ELISAs were performed with a single concentration of biotinylated reagent (bNAbs or CD4-Ig, as indicated) binding to JR-FL gp120 or CH505 SOSIP. The unlabeled competing mAbs or CD4-Ig were titrated into the ELISAs at increasing concentrations to evaluate the effect on biotinylated reagent binding.

Jia, M., Liberatore, R. A., Guo, Y., Chan, K. W., Pan, R., Lu, H., ... & Wu, X. (2020). VSV-displayed HIV-1 envelope identifies broadly neutralizing antibodies class-switched to IgG and IgA. Cell host & microbe, 27(6), 963-975.

Figure 4 Glycan influence on M4008_N1 neutralization.

Neutralization tests were carried out for M4008_N1 against glycan-modified Env variants for strains BG505 (c) and JR-FL (d). Note that in the case of BG505, removal of glycans next to the M4008_N1 binding site improved its neutralization potency, especially for glycans of N301 of the primary gp120 and N197 of the neighboring gp120, while in the case of JR-FL, introducing the glycan of N197 of the neighboring gp120 reduced its potency. Neutralization was performed in duplicate wells, and the data are represented as means.

Chan, K. W., Luo, C. C., Lu, H., Wu, X., & Kong, X. P. (2021). A site of vulnerability at V3 crown defined by HIV-1 bNAb M4008_N1. Nature communications, 12(1), 1-12.

Figure 5 Assessment of key residues at the interface between M4008_N1 and the Env trimer.

a, b Neutralization analyses of M4008_N1 against various mutated Env variants from strain BG505 (a) and JR-FL (b).

Chan, K. W., Luo, C. C., Lu, H., Wu, X., & Kong, X. P. (2021). A site of vulnerability at V3 crown defined by HIV-1 bNAb M4008_N1. Nature communications, 12(1), 1-12.

Figure 6 Assessment of key residues at the interface between M4008_N1 and the Env trimer.

c, d ELISA (c) and neutralization analyses (d) of M4008_N1 CDR H3 variants against BG505. Neutralization was performed in duplicate wells, and the data are represented as means. ELISA was performed in duplicate wells for three independent experiments, and the data shown are means ± SEM.

Chan, K. W., Luo, C. C., Lu, H., Wu, X., & Kong, X. P. (2021). A site of vulnerability at V3 crown defined by HIV-1 bNAb M4008_N1. Nature communications, 12(1), 1-12.

Figure 7 ELISA analysis of different single residue germline-reverted M4008_N1 variants.

Analysis was performed in duplicate wells for three independent experiments, and the data shown are means ± SEM.

Chan, K. W., Luo, C. C., Lu, H., Wu, X., & Kong, X. P. (2021). A site of vulnerability at V3 crown defined by HIV-1 bNAb M4008_N1. Nature communications, 12(1), 1-12.