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Originally published In Press as doi:10.1074/jbc.M111679200 on January 15, 2002

J. Biol. Chem., Vol. 277, Issue 13, 11292-11296, March 29, 2002
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Identification of a Common Sphingolipid-binding Domain in Alzheimer, Prion, and HIV-1 Proteins*

Radhia Mahfoud, Nicolas Garmy, Marc Maresca, Nouara Yahi, Antoine Puigserver, and Jacques FantiniDagger

From the Institut Méditerranéen de Recherche en Nutrition, Unité Mixte de Recherche-Institut National de la recherche Agronomique 1111, Faculté des Sciences St-Jérôme, 13397 Marseille Cedex 20, France

The V3 loop of the human immunodeficiency virus (HIV)-1 surface envelope glycoprotein gp120 is a sphingolipid-binding domain mediating the attachment of HIV-1 to plasma membrane microdomains (rafts). Sphingolipid-induced conformational changes in gp120 are required for HIV-1 fusion. Galactosylceramide and sphingomyelin have been detected in highly purified preparations of prion rods, suggesting that the prion protein (PrP) may interact with selected sphingolipids. Moreover, a major conformational transition of the Alzheimer beta -amyloid peptide has been observed upon interaction with sphingolipid-containing membranes. Structure similarity searches with the combinatorial extension method revealed the presence of a V3-like domain in the human prion protein PrP and in the Alzheimer beta -amyloid peptide. In each case, synthetic peptides derived from the predicted V3-like domain were found to interact with monomolecular films of galactosylceramide and sphingomyelin at the air-water interface. The V3-like domain of PrP is a disulfide-linked loop (Cys179-Cys214) that includes the E200K mutation site associated with familial Creutzfeldt-Jakob disease. This mutation abrogated sphingomyelin recognition. The identification of a common sphingolipid-binding motif in gp120, PrP, and beta -amyloid peptide underscores the role of lipid rafts in the pathogenesis of HIV-1, Alzheimer, and prion diseases and may provide new therapeutic strategies.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 33-491-288-761; Fax: 33-491-288-440; E-mail: jacques.fantini@univ.u-3mrs.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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