Abstract
We investigated the protein/protein interactions that occur during human immunodeficiency virus (HIV-1) budding. We evaluated the binding to Pr55Gag particles of peptides mapping to the cytoplasmic tail of gp41TM and of host-cell proteins, in a cell-free, in vitro assay. Host-cell proteins and irrelevant viral envelope peptides did not bind. Peptides corresponding to a large central domain of the gp41TM cytoplasmic tail (93 residues) bound to Pr55Gag particles. This demonstrates that a Gag/Env interaction is responsible for the specific incorporation of the Env glycoprotein into nascent HIV-1 virions, and defines more accurately the gp41TM domain involved in this interaction.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Cell Line
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Cell Membrane / ultrastructure
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Cell Membrane / virology
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Cricetinae
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Gene Products, gag / chemistry*
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Gene Products, gag / metabolism*
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HIV Envelope Protein gp41 / chemistry*
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HIV Envelope Protein gp41 / metabolism*
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HIV-1 / growth & development
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HIV-1 / physiology*
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HIV-1 / ultrastructure
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Humans
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Peptide Mapping
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Protein Precursors / chemistry*
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Protein Precursors / metabolism*
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Transfection
Substances
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Gene Products, gag
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HIV Envelope Protein gp41
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Peptide Fragments
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Protein Precursors
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p55 gag precursor protein, Human immunodeficiency virus 1