Provided is a HIV-1 neutralizing antibody (clone B-p1b5) that targets the CD4-binding site of Env. Both 426c WT Core and HxB2 WT Core could be immunoprecipitated by B-p1b5. B-p1b5 neutralized the WT 426c virus (IC50 of 32.05 μg/mL) expressed in GnTI−/− cells.
Figure 1 Trimeric Env-Binding and Neutralizing Properties of VRC01-like Antibodies Elicited by the 426c Core Germline-Targeting Immunogen.
The binding of eight VRC01-like antibodies generated following the prime immunization against (A) the autologous 426c WT DS-SOSIP; (B) its variant that lacks the N276, N460, and N463 NLGS (426c DS-SOSIP D3); (C) a variant that only lacks the N276 glycan (426c D276 DS-SOSIP); and (D) the heterologous 45_01dG5 NFL TD-2CC+(DS+), which also lacks the N276 NLGS, was measured using Biolayer interferometry.
Parks, K. R., MacCamy, A. J., Trichka, J., Gray, M., Weidle, C., Borst, A. J., Khechaduri, A., Takushi, B., Agrawal, P., Guenaga, J., Wyatt, R. T., Coler, R., Seaman, M., LaBranche, C., Montefiori, D. C., Veesler, D., Pancera, M., McGuire, A., & Stamatatos, L. (2019). Overcoming Steric Restrictions of VRC01 HIV-1 Neutralizing Antibodies through Immunization. Cell reports, 29(10), 3060–3072.e7.
Figure 2 Vaccine Elicited Antibodies Bind in to Env Core with Glycans at N276.
Following co-immunoprecipitation, 426c WT Core (left) and HxB2 WT Core (right) were washed and eluted from the beads.
Parks, K. R., MacCamy, A. J., Trichka, J., Gray, M., Weidle, C., Borst, A. J., Khechaduri, A., Takushi, B., Agrawal, P., Guenaga, J., Wyatt, R. T., Coler, R., Seaman, M., LaBranche, C., Montefiori, D. C., Veesler, D., Pancera, M., McGuire, A., & Stamatatos, L. (2019). Overcoming Steric Restrictions of VRC01 HIV-1 Neutralizing Antibodies through Immunization. Cell reports, 29(10), 3060–3072.e7.
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