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J Biol Chem, Vol. 273, Issue 34, 21988-21997, August 21, 1998

Identification of V3 Loop-binding Proteins as Potential Receptors Implicated in the Binding of HIV Particles to CD4⁺ Cells

Christian Callebaut, Julià Blanco, Nadia Benkirane^§, Bernard Krust, Etienne Jacotot, Gilles Guichard^§, Nabila Seddiki, Josette Svab, Elisabeth Dam, Sylviane Muller^§, Jean-Paul Briand^§, and Ara G. Hovanessian

From the  Unité de Virologie et Immunologie Cellulaire, ERS 572 CNRS, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15 and ^§ Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 15 rue Descartes, 67084 Strasbourg Cedex, France

The binding of human immunodeficiency virus (HIV) type 1 particles to CD4⁺ cells could be blocked either by antibodies against the V3 loop domain of the viral external envelope glycoprotein gp120, or by the V3 loop mimicking pseudopeptide 5[K(CH₂N)PR]-TASP, which forms a stable complex with a cell-surface-expressed 95-kDa protein. Here, by using an affinity matrix containing 5[K(CH₂N)PR]-TASP and cytoplasmic extracts from human CEM cells, we purified three V3 loop-binding proteins of 95, 40, and 30 kDa, which after microsequencing were revealed to be as nucleolin, putative HLA class II-associated protein (PHAP) II, and PHAP I, respectively. The 95-kDa cell-surface protein was also isolated and found to be nucleolin. We show that recombinant preparations of gp120 bind the purified preparations containing the V3 loop-binding proteins with a high affinity, comparable to the binding of gp120 to soluble CD4. Such binding is inhibited either by 5[K(CH₂N)PR]-TASP or antibodies against the V3 loop. Moreover, these purified preparations inhibit HIV entry into CD4⁺ cells as efficiently as soluble CD4. Taken together, our results suggest that nucleolin, PHAP II, and PHAP I appear to be functional as potential receptors in the HIV binding process by virtue of their capacity to interact with the V3 loop of gp120.

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