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PMID: 7707555 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Sphingolipid-dependent fusion of Semliki Forest virus with cholesterol-containing liposomes requires both the 3-hydroxyl group and the double bond of the sphingolipid backbone.

Journal of virology ·Vol. 69 ·No. 5 ·1995-05-00 ·Pages 3220-3

Corver J, Moesby L, Erukulla RK, Reddy KC, Bittman R, Wilschut J

Abstract

Low-pH-induced membrane fusion of Semliki Forest virus (SFV) in a model system is mediated by sphingolipids in the target membrane; ceramide is the sphingolipid minimally required (J. L. Nieva, R. Bron, J. Corver, and J. Wilschut, EMBO J. 13:2797-2804, 1994). Here, using various ceramide analogs, we demonstrate that sphingolipid-dependent fusion of SFV with cholesterol-containing liposomes exhibits remarkable molecular specificity, the 3-hydroxyl group and the 4,5-trans carbon-carbon double bond of the sphingosine backbone being critical for the sphingolipid to mediate the process. This observation supports the notion that sphingolipids act as a cofactor in SFV fusion, interacting directly with the viral fusion protein to induce its ultimate fusion-active conformation.

MeSH Terms
Ceramides/chemistry,physiology Cholesterol/chemistry Hydrogen-Ion Concentration Hydroxylation Liposomes/chemistry Membrane Fusion/physiology Models, Biological Molecular Structure Protein Conformation Semliki forest virus/physiology Sphingolipids/chemistry,physiology Viral Fusion Proteins/chemistry,physiology
Chemicals
Ceramides Liposomes Sphingolipids Viral Fusion Proteins Cholesterol
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Corver J
Department of Physiological Chemistry, Groningen Institute for Drug Studies, University of Groningen, The Netherlands.
Moesby L
Erukulla R K
Reddy K C
Bittman R
Wilschut J
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1995-05-00
Pages
3220-3
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC189029
Subset
IM
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