Mouse Anti-HIV-1 Recombinant Antibody (clone KEL10) (CAT#: FAMAB-0176CQ)

Figure 1 Generation of mAb KEL10.

Screening of cross-reacting monoclonal hybridomas generated against ELDKWA by ELISA. KEL10 was used for further studies due to its ability to secrete higher levels of antibody and also demonstrating higher cross-reactivity with different epitopes.

Bhowmick, A., & Salunke, D. M. (2012). Limited conformational flexibility in the paratope may be responsible for degenerate specificity of HIV epitope recognition. International immunology, 25(2), 77-90.

Figure 2 ELISA-based binding analysis of KEL10.

(A) Binding of pure KEL10 to immobilized immunizing peptide and its variants in ELISA, as a function of antibody concentration. A total of 2 μg of peptide–BSA conjugate was immobilized as antigen for ELISA. BSA was used as a control and the average background OD (optical density) at 490nm was 0.07. All the peptide epitopes demonstrated equivalent binding to KEL10. (B) Binding of KEL10 to gp41 using a clinical ELISA kit. KEL10 showed comparable binding to 4E10 and to the gp41 core protein coated in the ELISA plate (antibody concentration: 0.25 uM).

Bhowmick, A., & Salunke, D. M. (2012). Limited conformational flexibility in the paratope may be responsible for degenerate specificity of HIV epitope recognition. International immunology, 25(2), 77-90.

Figure 3 Generation of the peptide-bound structures of KEL10 Fv. R

MSDs of the Cα atoms of the CDRs and peptide (A) and that of the whole KEL10 Fv and the peptide (B) during the 6 ns MD simulations of each of the peptide-bound Fv structures. In each case, the averaged structure from the last 4 ns run was energy minimized and used for further analysis. All the epitopes were found to bind in the same binding pocket as shown in (C). Stereoscopic representation of the superimposition of the different peptides in the antibody-bound conformation is shown in (D). The trajectories of the different peptide-bound structures and the peptides are coloured according to the legend.

Bhowmick, A., & Salunke, D. M. (2012). Limited conformational flexibility in the paratope may be responsible for degenerate specificity of HIV epitope recognition. International immunology, 25(2), 77-90.