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Clinical Chemistry 45: 638-650, 1999;
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(Clinical Chemistry. 1999;45:638-650.)
© 1999 American Association for Clinical Chemistry, Inc.

Articles

Anti-Free Prostate-specific Antigen Monoclonal Antibody Epitopes Defined by Mimotopes and Molecular Modeling

Sandrine Michel1, Gilbert Deléage2, Jean-Philippe Charrier1, Jacques Passagot1, Nicole Battail-Poirot1, Geneviève Sibai1, Michel Jolivet1 and Colette Jolivet-Reynaud3,1

1 bioMérieux, Département R&D unité Immunoessais, Chemin de l'Orme, 69280 Marcy L'Etoile, France.

2 Institut de Biologie et de Chimie des Proteines, Unite Propre de Recherche, 412/Centre National de la Recherche Scientifique, 7 passage du Vercors, 69367 Lyon Cedex 07, France.

3 Unite Mixte de Recherche, 103 bioMérieux/Centre National de la Recherche Scientifique, ENS, 46 allée d'Italie, 69364 Lyon Cedex 07, France.

Background: Prostate-specific antigen (PSA) is an important marker for the diagnosis and management of prostate cancer, and the free PSA/total PSA ratio has been shown to be efficient for distinguishing prostate cancer from benign prostatic hyperplasia. We report here the characterization of seven mouse monoclonal antibodies (mAbs) and the partial localization of two conformational epitopes identified by anti-free PSA mAbs.

Methods: The mAbs were studied by competition and sandwich assays, and the epitope localization of the two anti-free PSA mAbs (6C8D8 and 5D3D11) was performed using phage displayed peptide libraries and molecular modeling.

Results: The seven mAbs were classified into three groups according to their recognition specificities and their ability to inhibit the enzymatic activity of PSA and the formation of PSA-{alpha}1-antichymotrypsin (ACT) complex. Among the anti-free PSA mAb group, 6C8D8 recognized the phage displayed peptide RKLRPHWLHFHPVAV, two parts of which presented similarities with two regions distant on the PSA sequence but joined in the tridimensional structure. mAb 5D3D11 recognized the peptide DTPYPWGWLLDEGYD, which is similar to a PSA region located on the board of the groove containing the PSA enzymatic site. Both epitopes were located in the theoretical ACT binding site described previously. Moreover, these mAbs were able to inhibit the enzymatic activity of PSA.

Conclusions: These epitope localizations are in agreement with the ability of both mAbs to inhibit enzymatic activity and ACT fixation. The results presented here could bring information for the generation of clinically relevant PSA assays.© 1999 American Association for Clinical Chemistry




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