Table 1.
A list of mAbs to BoNT/A with their epitopes and affinities for BoNT/A1, A2, and A3 as measured by dissociation rates (KDs).
Figure 1.
A graph indicating the % of inhibition in activity of BoNT/A1 or /A1 light chain following neutralization with the antibody panel.
The sample with no antibodies had no inhibition of activity, so the % of inhibition in activity is calculated by dividing the peak area ratio of the peptide cleavage product over the internal standard peptide of the individual antibody by the peak area ratio of the sample with no antibodies.
Table 2.
Peak area ratios of the peptide cleavage product over the internal standard peptide obtained from the Endopep-MS reaction of BoNT/A with its peptide substrate in the presence of the antibody panel.
Figure 2.
Mass spectra of the Endopep-MS BoNT/A1 reaction with either ING2 (2A) or CR2 (2B) antibodies.
The peptide cleavage product indicating BoNT/A1 is present in both cases at m/z 1197.7 and the internal standard is present at m/z 1204.7.
Figure 3.
Mass spectra of the Endopep-MS botulinum neurotoxin A reaction after extraction of the toxin with either CR2 (3A), ING2 (3B), or B4 (3C) antibodies.
The peptide cleavage product indicating the presence of BoNT/A is present in both cases at m/z 1197.7 and the internal standard is present at m/z 1204.7.
Table 3.
Peak area ratios of the peptide cleavage product over the internal standard peptide obtained from the Endopep-MS reaction of BoNT A after its extraction by the antibody panel.