Recombinant Human Anti-HIV-1 Antibody Fab Fragment (Fab2558) (CAT#: PABX-092-F (E))

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 Structural similarity of the antigen-binding sites of VH5-51 encoded anti-V3 mAbs.

(A) A structural superimposition of the Ca atoms of the Fab variable domains of complexes 1006/MN (green), 2219/MN (cyan), 2557/NY5 (magenta), 2558/MN (yellow), and 4025/ConA
(salmon). Note the domains of CDR H1, H2, L1 and L2 superimposed well, while that of CDR L3 and H3 is more structurally divergent. (B) Same superimposition as that in panel (A) but with the key contact residues of the mAbs labeled (all contact residues are shown in Tables 4 and 5). The position of the V3 is illustrated as a dashed line. (C) and (D) Structural details of the antigen combining sites of the light (C) and heavy chains (D) in the five complexes.

Gorny, M. K., Sampson, J., Li, H., Jiang, X., Totrov, M., Wang, X. H., ... & Cardozo, T. (2011). Human anti-V3 HIV-1 monoclonal antibodies encoded by the VH5-51/VL lambda genes define a conserved antigenic structure. PloS one, 6(12), e27780.