Recombinant mouse antibody to gp41. T26 was found to predominantly bind to oligomeric gp41 and not to monomeric gp41. Binding of this Ab to H9/IIIB-infected cells gave a weak signal which was slightly increased by sCD4 pretreatment.
Figure 1 WB analysis of mAbs. Each WB strip was incubated with 20 µl sera, 32 µg T26 mAb or 4 µg other mAbs diluted with 2 ml wash solution.
The
healthy volunteer sera as negative control and AIDS patient sera as positive
control reference were performed.
Guenaga, J., Dosenovic, P., Ofek, G., Baker, D., Schief, W. R., Kwong, P. D., ... & Wyatt, R. T. (2011). Heterologous Epitope-Scaffold Prime∶ Boosting Immuno-Focuses B Cell Responses to the HIV-1 gp41 2F5 Neutralization Determinant. PloS one, 6(1).
Figure 4 The temperature dependency of MAb T26 binding.
MAb T26 binding to H9/IIIB at 37 C was higher than at 4 C.
Usami, O., Xiao, P., Ling, H., & Hattori, T. (2006). Competitive Study of Monoclonal Antibodies against the HIV‐1 Gp41 Core Structure. Microbiology and immunology, 50(2), 131-134.
Figure 5 The decreased binding of biotinylated MAb 50.69, 98.6, or T26 to H9/IIIB cells after preincubation with MAb 50.69 (open bars), 98.6 (filled bars), or hIgG (gray bars).
The negative control was calculated as the MFI without preincubation MAb and with biotinylated MAb.
Usami, O., Xiao, P., Ling, H., & Hattori, T. (2006). Competitive Study of Monoclonal Antibodies against the HIV‐1 Gp41 Core Structure. Microbiology and immunology, 50(2), 131-134.
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