Recombinant Mouse Anti-HPV Major capsid protein L1 Antibody (H16.U4 ) (CAT#: PABL-199)

Figure 1 Binding of 16 and 52 specific MAbs to VLPs with mutations of the BC loop. VLPs 16:wt (▪), 16:BC (□), 52:wt (•), and 52:BC (○) were titrated across a plate and reacted with CAMVIR-1, H16.V5, H16.E70, H52.B9, and H52.D12 in an ELISA.

Carter, J. J., Wipf, G. C., Benki, S. F., Christensen, N. D., & Galloway, D. A. (2003). Identification of a human papillomavirus type 16-specific epitope on the C-terminal arm of the major capsid protein L1. Journal of virology, 77(21), 11625-11632.

Figure 2 Binding of MAbs to HPV-16/31 hybrid VLPs.

MAbs were tested by ELISA for reactivity to HPV-16 and HPV-31 wild-type VLPs and mutated VLPs that are indicated on the x-Axis. The y-axis are normalized optical density values (see text) for H16.V5 (solid), H16.E70 (striped), H16.U4 (cross-hatched), and H31.A6 (opposite striped) binding.

Carter, J. J., Wipf, G. C., Benki, S. F., Christensen, N. D., & Galloway, D. A. (2003). Identification of a human papillomavirus type 16-specific epitope on the C-terminal arm of the major capsid protein L1. Journal of virology, 77(21), 11625-11632.

Figure 3 Identification of residues on the FG loop important for MAb binding.

The sequence of HPV-16 and HPV-31 L1 are compared (A). Residues that are predicted to be>45% surface accessible are indicated with arrows and bold type is used to indicate nonconserved residues. CAMVIR-1, H16.V5, H16.E70, and H16.U4 were tested for binding to VLPs that were serially diluted prior to testing. The normalized binding values are presented (B), with each MAb represented by bars.

Carter, J. J., Wipf, G. C., Benki, S. F., Christensen, N. D., & Galloway, D. A. (2003). Identification of a human papillomavirus type 16-specific epitope on the C-terminal arm of the major capsid protein L1. Journal of virology, 77(21), 11625-11632.