Abstract
Using an inhibitory synthetic peptide (DP-178) from HIV-1 gp41, we have trapped HIV-1 envelope glycoprotein (Env) undergoing conformational changes during virus entry. Our data show that DP-178 binds gp41 and inhibits Env-mediated membrane fusion after gp120 interacts with cellular receptors, indicating that conformational changes involving the coiled coil domain of gp41 are required for entry. Capture of this fusion-active conformation of Env provides insights into the early events leading to Env-mediated membrane fusion.
MeSH terms
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3T3 Cells
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Amino Acid Sequence
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Animals
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Anti-HIV Agents / pharmacology
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Cell Fusion / drug effects
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Cell Line
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Enfuvirtide
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HIV Envelope Protein gp41 / chemistry*
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HIV Envelope Protein gp41 / metabolism*
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HIV Envelope Protein gp41 / pharmacology
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HIV-1 / drug effects
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HIV-1 / physiology*
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Humans
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Membrane Fusion / drug effects
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Membrane Fusion / physiology*
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Mice
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Models, Biological
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / pharmacology
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Protein Conformation*
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Receptors, Chemokine / drug effects
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Receptors, Chemokine / physiology
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Receptors, HIV / drug effects
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Receptors, HIV / physiology
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Transfection
Substances
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Anti-HIV Agents
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HIV Envelope Protein gp41
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Peptide Fragments
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Receptors, Chemokine
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Receptors, HIV
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Recombinant Fusion Proteins
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Enfuvirtide