Anti-HIV-1 antibody is a Human of Fab class that binds to an HIV-1. This antibody was originally selected for binding to a V3 fusion protein and can neutralize primary isolates from subtypes B, A, and F. Thus, it represents a cross-reactive, human anti-V3 antibody. It developed From a human immunodeficiency virus type 1-infected individual.
Figure 1 Measurement of Env incorporation by Western blot.
WT and mutant viruses were produced in transfected 293T cells, lysed, and analyzed by SDS-PAGE (4±20%) and Western blot. An anti-gp120 MAb cocktail (V3: 391/95-D, 694/98-D, 2219, 2558; C2: 847-D, 1006-30D; C5: 450-D, 670-D) and a p24 Gag MAb (91±5) were used to detect the relative levels of Env and Gag associated with virions. The ratios of Env/Gag were calculated.
Upadhyay, C., Feyznezhad, R., Yang, W., Zhang, H., Zolla-Pazner, S., & Hioe, C. E. (2018). Alterations of HIV-1 envelope phenotype and antibody-mediated neutralization by signal peptide mutations. PLoS pathogens, 14(1), e1006812.
Figure 2 Reactivities of MAbs with V3 peptides by ELISA.
The binding curves for anti-V3 MAbs 2219 and 447-52D are shown with filled squares and triangles, respectively. Data for the human anti-parvovirus B19 MAb 1418, used as a negative control, are shown as open circles. O.D., optical density; *, value obtained by extrapolation because the binding curve did not reach the saturation point; NR, not reactive.
Stanfield, R. L., Gorny, M. K., Zolla-Pazner, S., & Wilson, I. A. (2006). Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity. Journal of virology, 80(12), 6093-6105.
Figure 3 The neutralization of nine HIV-1 pseudoviruses by mAb 2191 using U87 as target cells.
The neutralization curves of anti-V3 mAb 2191 against nine selected HIV-1 pseudoviruses are shown with their corresponding AUC and IC50 values. Fifty percent neutralization is denoted
by the dashed line. Significant neutralization at the confidence level of p,0.001 (denoted with * after AUC values) was determined statistically based on comparison with the AUC values of the negative controls together with the slopes of the titration curves as described in Materials and Methods.
For viruses coming from patients where the date of infection is known, viruses are denoted as coming from acutely- or chronically-infected patients,
and the clade of the virus is denoted by the capital letter in its name (A, B, C or D).
doi:10.1371/journal.pone.0010254.g001
Hioe, C. E., Wrin, T., Seaman, M. S., Yu, X., Wood, B., Self, S., ... & Zolla-Pazner, S. (2010). Anti-V3 monoclonal antibodies display broad neutralizing activities against multiple HIV-1 subtypes. PloS one, 5(4), e10254.
Figure 4 Cα traces of the Fab 2219-peptide complexes.
(a) Fab 2219 plus MN peptide; (b) Fab 2219 plus UG1033 peptide; (c) Fab 2219 plus UR29 peptide. In all panels, the peptide is colored in red; Fab light and heavy chains in light and dark gray, respectively; and the Fab CDR loops L1 in orange, L2 in dark purple, L3 in green, H1 in light blue, H2 in pink, and H3 in yellow. Images were produced using Molscript, Bobscript, and Raster3D.
Stanfield, R. L., Gorny, M. K., Zolla-Pazner, S., & Wilson, I. A. (2006). Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity. Journal of virology, 80(12), 6093-6105.
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