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From:
doi: 10.1128/JVI.01941-12

Fig 3

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Unidirectional competition by HMAbs to aa 412 to 423 and aa 434 to 446 for binding to E2. (A) Epitope locations of the selected antigenic domain B and D HMAbs in aa 434 to 446 and in other discontinuous regions on E2. (B and C) Cross-competition studies with HC33 HMAbs and either antigenic domain B or D HMAbs. Cell lysates of HEK 293T cells expressing 1a H77C E1E2 were employed. An irrelevant antibody (R04) and no antibody were used as negative controls. (B) Unlabeled HC33 HMAbs were used to compete against the corresponding biotinylated HC33 HMAbs to define maximum competition (Self). Unlabeled HC84 or HC-11 HMAb at 50 μg/ml (x axis) was incubated with E2 that had been immobilized on a GNA-precoated ELISA plate. Biotinylated HC33 HMAbs at 2 μg/ml were then added, and bound biotinylated HMAbs were measured with AP-conjugated streptavidin. (C) Unlabeled HC84 HMAbs were used to compete against the corresponding biotinylated HC84 HMAbs to define maximum competition (Self). Unlabeled HC33 HMAbs at 50 μg/ml (x axis) were incubated with E2 that had been immobilized on a GNA-precoated ELISA plate. Biotinylated HC84 HMAbs at 1 μg/ml were then added, and bound biotinylated HMAbs were measured with AP-conjugated streptavidin. Data for panels B and C are the mean values of two experiments performed in triplicate.

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