Abstract
Specific interactions between envelope and core proteins govern the membrane assembly of most enveloped viruses. Despite this, mixed infections lead to pseudotyping, the association of the viral cores of one virus with the envelopes of another. How does this occur? We show here that the detergent-insoluble lipid rafts of the plasma membrane function as a natural meeting point for the transmembrane and core components of a phylogenetically diverse collection of enveloped viruses. As a result, viral particles preferentially incorporate both the envelope components of other viruses as well as the extra- and intracellular constituents of host cell lipid rafts, including gangliosides, glycosyl phosphatidylinositol-anchored surface proteins, and intracellular signal transduction molecules. Pharmacological disruption of lipid rafts interferes with virus production.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Animals
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Antigens, CD / metabolism
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Cell Fractionation
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Cell Line, Transformed
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Cholesterol / metabolism
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Detergents
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G(M1) Ganglioside / metabolism
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GRB2 Adaptor Protein
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Human T-lymphotropic virus 1 / metabolism
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Humans
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Membrane Microdomains / metabolism*
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Mice
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Moloney murine leukemia virus / metabolism
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Octoxynol
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Proteins / metabolism
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Proto-Oncogene Proteins pp60(c-src) / metabolism
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Solubility
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Viral Core Proteins / metabolism*
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Viral Envelope Proteins / metabolism*
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Virion / metabolism
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Virus Assembly
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ras Proteins / metabolism
Substances
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Adaptor Proteins, Signal Transducing
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Antigens, CD
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Detergents
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GRB2 Adaptor Protein
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GRB2 protein, human
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Grb2 protein, mouse
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Proteins
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Viral Core Proteins
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Viral Envelope Proteins
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G(M1) Ganglioside
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Octoxynol
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Cholesterol
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Proto-Oncogene Proteins pp60(c-src)
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ras Proteins