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Originally published In Press as doi:10.1074/jbc.M202255200 on April 2, 2002

J. Biol. Chem., Vol. 277, Issue 24, 21776-21785, June 14, 2002
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Sphingomyelin and Cholesterol Promote HIV-1 gp41 Pretransmembrane Sequence Surface Aggregation and Membrane Restructuring*

Asier Sáez-CiriónDagger §, Shlomo Nir, Maier LorizateDagger §, Aitziber AgirreDagger §, Antonio Cruz||**, Jesús Pérez-Gil||, and José L. NievaDagger Dagger Dagger

From the Dagger  Unidad de Biofísica (Centro Superior de Investigaciones Científicas-Universidad del País Vasco) and Departamento de Bioquímica, Universidad del País Vasco, Apartado 644, 48080 Bilbao, Spain, the  Seagram Center for Soil and Water Sciences, Faculty of Agricultural, Food and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel, and the || Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense de Madrid, 28040 Madrid, Spain

The interfacial sequence DKWASLWNWFNITNWLWYIK, preceding the transmembrane anchor of gp41 glycoprotein subunit, has been shown to be essential for fusion activity and incorporation into virions. HIVc, a peptide representing this region, formed lytic pores in liposomes composed of the main lipids occurring in the human immunodeficiency virus, type 1 (HIV-1), envelope, i.e. 1-palmitoyl-2-oleoylphosphatidylcholine (POPC):sphingomyelin (SPM):cholesterol (Chol) (1:1:1 mole ratio), at low (>1:10,000) peptide-to-lipid mole ratio, and promoted the mixing of vesicular lipids at >1:1000 peptide-to-lipid mole ratios. Inclusion of SPM or Chol in POPC membranes had different effects. Whereas SPM sustained pore formation, Chol promoted fusion activity. Even if partitioning into membranes was not affected in the absence of both SPM and Chol, HIVc had virtually no effect on POPC vesicles. Conditions described to disturb occurrence of lateral separation of phases in these systems reproduced the high peptide-dose requirements for leakage as found in pure POPC vesicles and inhibited fusion. Surface aggregation assays using rhodamine-labeled peptides demonstrated that SPM and Chol promoted HIVc self-aggregation in membranes. Employing head-group fluorescent phospholipid analogs in planar supported lipid layers, we were able to discern HIVc clusters associated to ordered domains. Our results support the notion that the pretransmembrane sequence may participate in the clustering of gp41 monomers within the HIV-1 envelope, and in bilayer architecture destabilization at the loci of fusion.

* This work was supported in part by Dirección General de Ciencia y Tecnología Grants PB96-0171 and BIO2000-0929, by Basque Government Grants EX-1998-28 and PI-1998-32, and by University of the Basque Country Grants UPV 042.310-EA085/97 and UPV 042.310-G03/98.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.

§ Recipient of a predoctoral fellowship from the Basque Government.

** Recipient of a postdoctoral fellowship from Community of Madrid.

Dagger Dagger To whom correspondence should be addressed. Tel.: 34-94-601-2615; Fax: 34-94-464-8500; E-mail: gbpniesj@lg.ehu.es.

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