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. Author manuscript; available in PMC: 2009 Feb 15.
Published in final edited form as: Bioorg Med Chem. 2007 Nov 5;16(4):1903–1913. doi: 10.1016/j.bmc.2007.11.001

Table II.

Fab neutralization potency and possible PA interaction domains. Antibody PA neutralization potency was determined in an antibody dose dependent protection assay with lower and higher challenge approaches as stated in the text. In a lower challenge assay, antibody is pre-incubated with PA, added to the RAW264.7 cells, and then LF is applied for the MTT assay. In the higher challenge assay, antibody, PA and LF are mixed and immediately applied to the RAW264.7 cells for the MTT assay. The possible epitopes on PA are defined by a neutralizing antibody as deduced via the assay.

Fab Neutralization Potency (IC) Possible Epitope on PA
A8 a65% at 400 μg/mL, 50% at 110 μg/mL Domain 1’, LF binding site
b54% at 400 μg/mL, 50% at 300 μg/mL
F1 a100% at 400 μg/mL, 50% at .25μg/mL Domain 4, ATR binding site
b80% at 400 μg/mL, 50% at 58 μg/mL
G11c a80% at 400 μg/mL, 50% at 60 μg/mL Domain 4, ATR binding site
G12c a29% at 400 μg/mL Domain 4, ATR binding site
a

Lower challenge assay;

b

Higher challenge assay;

c

Lower challenge assay only