Fig. 3.
Fig. 3. Inhibition of anti-hMOR antibody binding to hMOR by hMOR EL peptides. / Affinity-purified anti-hMOR IgG samples from individual healthy donors were incubated with or without 20 μg/mL peptide for 1 hour at 37°C and then added to recombinant hMOR/CHO cells for 45 minutes at 4°C. Antibody binding was assessed by cytofluorometry using biotin-labeled, goat anti-human IgG F(ab′)2–specific antibodies and PE-labeled streptavidin. Histograms show inhibition of the binding of affinity-purified anti-hMOR IgG prepared from samples from 7 healthy women (upper panel) and 7 healthy men (lower panel) to recombinant hMOR/CHO cells when incubated with hMOR EL1 peptide (■), hMOR EL3 peptide (░), and 70-86 MBP peptide (▪). The percentage of inhibition of IgG binding was calculated as follows:1−MFIin the presence of peptide−backgroundMFIin the absence of peptide (PBS)−background×100The background corresponded to the staining of recombinant hMOR/CHO cells obtained by using revealing reagents alone.

Inhibition of anti-hMOR antibody binding to hMOR by hMOR EL peptides.

Affinity-purified anti-hMOR IgG samples from individual healthy donors were incubated with or without 20 μg/mL peptide for 1 hour at 37°C and then added to recombinant hMOR/CHO cells for 45 minutes at 4°C. Antibody binding was assessed by cytofluorometry using biotin-labeled, goat anti-human IgG F(ab′)2–specific antibodies and PE-labeled streptavidin. Histograms show inhibition of the binding of affinity-purified anti-hMOR IgG prepared from samples from 7 healthy women (upper panel) and 7 healthy men (lower panel) to recombinant hMOR/CHO cells when incubated with hMOR EL1 peptide (■), hMOR EL3 peptide (░), and 70-86 MBP peptide (▪). The percentage of inhibition of IgG binding was calculated as follows:
1−MFIin the presence of peptide−backgroundMFIin the absence of peptide (PBS)−background×100
The background corresponded to the staining of recombinant hMOR/CHO cells obtained by using revealing reagents alone.
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