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Papers In Press, published online ahead of print January 15, 2002
Biochemistry and Nutrition, Faculty of Sciences St-Jerome, Marseille 13397 Cedex 20
Corresponding Author: j.fantini{at}caramail.com
The V3 loop of the 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.
J. Biol. Chem, 10.1074/jbc.M111679200
Submitted on December 7, 2001
Revised on January 14, 2002
Accepted on January 14, 2002
Identification of a common sphingolipid-binding domain in Alzheimer, prion and HIV-1 proteins
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