A combination of broadly neutralizing HIV-1 monoclonal antibodies targeting distinct epitopes effectively neutralizes variants found in early infection
L Goo, Z Jalalian-Lechak, BA Richardson… - Journal of …, 2012 - Am Soc Microbiol
Journal of virology, 2012•Am Soc Microbiol
Neutralizing antibody protection against HIV-1 may require broad and potent antibodies
targeting multiple epitopes. We tested 7 monoclonal antibodies (MAbs) against 45 viruses of
diverse subtypes from early infection. The CD4 binding site MAb NIH45-46W was most
broad and potent (91% coverage; geometric mean 50% inhibitory concentration [IC50], 0.09
μg/ml). Combining NIH45-46W and a V3-specific MAb, PGT128, neutralized 96% of viruses,
while PGT121, another V3-specific MAb, neutralized the remainder. Thus, 2 or 3 antibody …
targeting multiple epitopes. We tested 7 monoclonal antibodies (MAbs) against 45 viruses of
diverse subtypes from early infection. The CD4 binding site MAb NIH45-46W was most
broad and potent (91% coverage; geometric mean 50% inhibitory concentration [IC50], 0.09
μg/ml). Combining NIH45-46W and a V3-specific MAb, PGT128, neutralized 96% of viruses,
while PGT121, another V3-specific MAb, neutralized the remainder. Thus, 2 or 3 antibody …
Abstract
Neutralizing antibody protection against HIV-1 may require broad and potent antibodies targeting multiple epitopes. We tested 7 monoclonal antibodies (MAbs) against 45 viruses of diverse subtypes from early infection. The CD4 binding site MAb NIH45-46W was most broad and potent (91% coverage; geometric mean 50% inhibitory concentration [IC50], 0.09 μg/ml). Combining NIH45-46W and a V3-specific MAb, PGT128, neutralized 96% of viruses, while PGT121, another V3-specific MAb, neutralized the remainder. Thus, 2 or 3 antibody specificities may prevent infection by most HIV-1 variants.
American Society for Microbiology