Prostate-specific antigen (PSA) is a widely used marker for screening
and monitoring prostate cancer, We identified and characterized the ep
itopes of two anti-PSA monoclonal antibodies (mAbs) designated B80 and
B87. The epitopes were initially mapped as nonoverlapping by developi
ng a sandwich immunoassay to measure PSA with the two anti-PSA mAbs, T
he two antibodies do not cross-react with homologous pancreatic kallik
rein, but recognize epitopes unique to PSA, B80 and B87 can recognize
both free and complexed PSA. and hence measure total PSA. Epitope scan
ning and bacteriophage peptide library affinity selection procedures w
ere used to identify and locate an epitope on PSA, A possible epitope
for B80 was identified as being located on or near PSA amino acid resi
dues 50-58 (-GRH-SLFHP-), The epitope for B87 was likely on an exposed
nonlinear conformational determinant, unique to PSA, and not masked b
y the binding of B80 or alpha(1)-antichymotrypsin.