Recombinant Human Anti-HIV-1 Antibody Fab Fragment (2G12) (CAT#: PABX-087-F (E))

Figure 1 Processing of anti-HIV-2 mAbs by N. benthamiana PLCPs.

mAb 2F5 or 2G12 (200 ng) was incubated with NbALP (50 ng), NbCathB (51 ng) or with no enzyme added (control) for the indicated times and then analysed by immunoblotting with antibodies to the heavy chain of human IgG. The migration positions of selected m

Niemer, M., Mehofer, U., Verdianz, M., Porodko, A., Schähs, P., Kracher, D., ... & Mach, L. (2016). Nicotiana benthamiana cathepsin B displays distinct enzymatic features which differ from its human relative and aleurain-like protease. Biochimie, 122, 119-125.

Figure 2 Staining of 2G12 mAb and 9205 mAb on MT-4 cells 4 days after infection with HIV-1 strain NL4.4, HE, MN, and NDK.

MFI of the background fluorescence (blue histograms), for the 2G12 mAb binding (red histograms) and for the 9206 mAb binding (green histograms) are indicated.

Huskens, D., Van Laethem, K., Vermeire, K., Balzarini, J., & Schols, D. (2007). Resistance of HIV-1 to the broadly HIV-1-neutralizing, anti-carbohydrate antibody 2G12. Virology, 360(2), 294-304.

Figure 3 Ribbon diagrams showing the N-glycosylation site mutations (red balls) in gp120 of 2G12 mAb-exposed HIV-1 strains (left panel, 3 mutations) and the mannose-binding plant lectin-exposed HIV-1 strains (right panel, 15 mutations).

The left panel shows the 24 putative glycosylation sites represented by yellow circles and their accompanying amino acid number. The red circles indicate the deleted N-glycosylation sites that appear under 2G12 mAb in the 4 different HIV-2 isolates.
The rȔ

Huskens, D., Van Laethem, K., Vermeire, K., Balzarini, J., & Schols, D. (2007). Resistance of HIV-1 to the broadly HIV-1-neutralizing, anti-carbohydrate antibody 2G12. Virology, 360(2), 294-304.