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Ligands binding to distinct epitopes on the same target molecule may influence each other, for example, inhibiting binding to adjacent epitopes.
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The following nmAbs were involved in passive immunization studies yielding complete protection: 2G12, which binds to mannose residues on gp120 [23]; b12 or F105, antibodies against the CD4 binding site (CD4bs) [25], [25]; as well as 4E10 and 2F5, which bind to adjacent epitopes in the membrane proximal external region (MPER) of gp41 [26].
Recently, it has been found, however, that distinct monoclonal antibodies directed to adjacent epitopes in the distal domain of the extracellular moiety of PECAM, stimulate binding of each other, both in cell culture and in vivo.
Such competition assays are complicated by steric hindrance between Abs binding physically adjacent epitopes as well as more subtle positive and negative conformational effects that occur upon Ig binding to HA (Lubeck and Gerhard, 1982).
The high-density peptide microarray-based epitope mapping revealed clear binding to several adjacent peptides and epitopes for all three antibodies.
The layer formation seems to hinder aPL binding to β2GPI epitopes close to D5 [16].
Epitope mapping was performed with all antibodies to verify binding to linear epitopes.
ICR65, however, cross-reacted with mAbs binding to both epitopes.
The competitive inhibition of binding to overlapping epitopes has been described for antibodies to ACE.
Ligands binding to distinct epitopes of anchoring molecules may enter cells differently.
In Western blots performed with α-Sho86 100 antisera, Sho signal increased following treatment with PNGaseF, suggesting that N-glycosylation at Asn107 partially occludes antibody binding at the adjacent epitope for the peptide-directed antiserum.
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