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Volume 272, Number 11, Issue of March 14, 1997 pp. 7159-7166
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Pseudopeptide TASP Inhibitors of HIV Entry Bind Specifically to a 95-kDa Cell Surface Protein

(Received for publication, August 8, 1996, and in revised form, November 14, 1996)

Christian Callebaut Dagger , Etienne Jacotot Dagger , Bernard Krust Dagger , Gilles Guichard § , Julià Blanco Dagger , Agustin Valenzuela Dagger , Josette Svab Dagger , Sylviane Muller § , Jean-Paul Briand § and Ara G. Hovanessian Dagger

From the Dagger  Unité de Virologie et Immunologie Cellulaire, URA 1157 CNRS, Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris Cedex 15 and the § Institut de Biologie Moleculaire et Cellulaire, UPR 9021 CNRS, 15 rue Descartes, 67084 Strasbourg Cedex, France

The template assembled synthetic peptide constructs (TASP), pentavalently presenting the tripeptide KPR or RPK, are potent and specific inhibitors of human immunodeficiency virus (HIV) infection by preventing viral entry into permissive cells. Here the 5[KPsi (CH2N)PR]-TASP construct, Psi (CH2N) for reduced peptide bond, was used in studies to demonstrate its specific binding to a 95-kDa cell surface protein ligand. Compared to its nonreduced 5[KPR]-TASP counterpart, the pseudopeptide 5[KPsi (CH2N)PR]-TASP manifested higher affinity to bind to its cell surface ligand, increased activity to inhibit HIV infection, and resistance to degradation when incubated in serum from an HIV-1 seropositive individual. In ligand blotting experiments, the biotin-labeled 5[KPsi (CH2N)PR]-TASP identified a single 95-kDa protein in crude cell extracts. This 95-kDa protein (p95) is expressed on the cell surface since surface iodination of cells resulted in its labeling, and moreover, following incubation of cells with the biotin-labeled 5[KPsi (CH2N)PR]-TASP, the p95·TASP complex was recovered by affinity chromatography using avidin-agarose. All anti-HIV TASP constructs but not their control derivatives affected the binding of biotin-labeled 5[KPsi (CH2N)PR]-TASP to p95, thus emphasizing the specific nature of this binding. Since 5[KPsi (CH2N)PR]-TASP does not interact with HIV-envelope glycoproteins, our results suggest that TASP inhibitors mediate directly or indirectly a block in HIV-mediated membrane fusion process by binding to the cell surface expressed p95.


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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.