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J Biol Chem, Vol. 274, Issue 4, 2038-2044, January 22, 1999
, and
From the Cell Biology Programme During the budding of enveloped viruses from the
plasma membrane, the lipids are not randomly incorporated into the
envelope, but virions seem to have a lipid composition different from
the host membrane. Here, we have analyzed lipid assemblies in three different viruses: fowl plague virus (FPV) from the influenza virus
family, vesicular stomatitis virus (VSV), and Semliki Forest virus
(SFV). Analysis of detergent extractability of proteins, cholesterol,
phosphoglycerolipids, and sphingomyelin in virions showed that FPV
contains high amounts of detergent-insoluble complexes, whereas such
complexes are largely absent from VSV or SFV. Cholesterol depletion
from the viral envelope by methyl-
Structural Biology
Programme, European Molecular Biology Laboratory, Postfach 10 2209, D-69012 Heidelberg, Germany and Max-Planck-Institute for Molecular Cell
Biology and Genetics, Dresden 01307, Germany
-cyclodextrin results in increased
solubility of sphingomyelin and of the glycoproteins in the FPV
envelope. This biochemical behavior suggests that so-called raft-lipid
domains are selectively incorporated into the influenza virus envelope.
The "fluidity" of the FPV envelope, as measured by the fluorescence
polarization of diphenylhexatriene, was significantly lower than
compared with VSV or SFV. Furthermore, influenza virus hemagglutinin
incorporated into the envelope of recombinant VSV was largely
detergent-soluble, indicating the depletion of raft-lipid assemblies
from this membrane. The results provide a model for lipid selectivity
during virus budding and support the view of lipid rafts as
cholesterol-dependent, ordered domains in biological membranes.
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