Recombinant Mouse Anti-DENV E-DIII Antibody Fab Fragment (1A1D-2) (CAT#: PFBC-031)

Figure 1 Characteristics of DIII-specific MAbs used in this study

Sukupolvi-Petty, S., Austin, S. K., Purtha, W. E., Oliphant, T., Nybakken, G. E., Schlesinger, J. J., ... & Diamond, M. S. (2007). Type-and subcomplex-specific neutralizing antibodies against domain III of dengue virus type 2 envelope protein recognize adjacent epitopes. Journal of virology, 81(23), 12816-12826.

Figure 2 Flow cytometry histograms of mAbs binding to yeast expressing wild-type or mutant domain III.

The following antibodies were used as negative and positive staining controls, respectively, for each of the indicated yeast based on data from a prior publication ( Sukupolvi-Petty et al., 2007 ): wild-type, WNV E16 and 3H5-1; K305E, 1A1D-2 and 3H5-1; K307C, 1A1D-2 and 3H5-1; K310E, 1A1D-2 and 3H5-1; P384A, 3H5-1 and 5A2-7; G330D, 6B6-10 and 3H5-1. In each case, staining with 9F12 is shown in red. The data are representative of three independent experiments.

Rajamanonmani, R., Nkenfou, C., Clancy, P., Yau, Y. H., Shochat, S. G., Sukupolvi-Petty, S., ... & Lescar, J. (2009). On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes. Journal of General Virology, 90(4), 799-809.

Figure 3 Fab 1A1D-2:DENV complex formation is temperature dependent.

(a) DENV with no antibody. (b) DENV incubated with Fab 1A1D-2 at room temperature showed few particles with bound Fab molecules. (c) DENV incubated with Fab 1A1D-2 at 37 °C showed that most particles were saturated with Fab molecules.

Lok, S. M., Kostyuchenko, V., Nybakken, G. E., Holdaway, H. A., Battisti, A. J., Sukupolvi-Petty, S., ... & Diamond, M. S. (2008). Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins. Nature structural & molecular biology, 15(3), 312.