Important note: Information in this article was accurate in 1994. The state of the art may have changed since the publication date.
Characterization of a monoclonal antibody produced in an attempt to mimic the active site of HIV aspartyl protease using haptens based on inhibitor models.
J Immunol Methods. 1994 Aug 1;173(2):139-47. Unique Identifier : AIDSLINE MED/94321800 Hanin V; Campagne JM; Dominice C; Mani JC; Dufour MN; Jouin P; Pau B; Immunoanalyse et Innovation en Biologie Clinique, CNRS UMR 9921,; Faculte de Pharmacie, Montpellier, France.
Abstract:
The high binding affinity and specificity of antibodies for a great variety of ligands has been widely exploited in structure-activity relationship studies of biomolecules and more recently in the development of new catalysts for several chemical reactions. It is assumed that antibodies generated against haptenic protease inhibitors would recognize both these haptens and the substrate of the model proteolytic reaction. We have produced antibodies against HIV PRp12 aspartyl protease substrate analogues, chemically modified at the scissile bond, Phe-Pro. Identical chemical modifications have been reported for related HIV protease inhibitors. We finally selected an anti-hapten monoclonal antibody that specifically recognized the substrate and those haptens with both the phenylalanyl side chain and the prolyl pyrrolidine ring. This selectivity of recognition suggests that such an antibody might mimic the catalytic site of the model protease.
Keywords: Amino Acid Sequence Animal Antibodies, Monoclonal/BIOSYNTHESIS/*IMMUNOLOGY Antibody Specificity Binding, Competitive Chromatography, Affinity Cross Reactions Enzyme-Linked Immunosorbent Assay Haptens/CHEMISTRY/*IMMUNOLOGY Hybridomas HIV/*ENZYMOLOGY/IMMUNOLOGY HIV Protease/CHEMISTRY/*IMMUNOLOGY HIV Protease Inhibitors/CHEMISTRY/*IMMUNOLOGY Immune Sera/IMMUNOLOGY Mice Mice, Inbred BALB C Molecular Sequence Data Peptide Fragments/CHEMISTRY/IMMUNOLOGY Support, Non-U.S. Gov't JOURNAL ARTICLE
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