Abstract
HIV-1 release requires a direct interaction between the p6 domain of the Gag protein and Tsg101, a component of the cellular endosomal sorting complex required for transport I (ESCRT-I). Disruption of the binding between Gag and Tsg101 is highly detrimental to particle release, making this viral-host cell interaction a potential target for the development of novel anti-HIV-1 agents. An article in this issue reports on the application of a bacterial reverse two-hybrid strategy to identify a cyclic peptide that disrupts Gag-Tsg101 binding and suppresses HIV-1 particle release.
MeSH terms
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DNA-Binding Proteins / antagonists & inhibitors*
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DNA-Binding Proteins / metabolism
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Endosomal Sorting Complexes Required for Transport
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Endosomes / metabolism
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HIV-1 / drug effects*
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HIV-1 / physiology*
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Humans
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Models, Biological
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Peptides, Cyclic / pharmacology*
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Protein Binding / drug effects
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Transcription Factors / antagonists & inhibitors*
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Transcription Factors / metabolism
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Vesicular Transport Proteins / drug effects
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Vesicular Transport Proteins / metabolism
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gag Gene Products, Human Immunodeficiency Virus / antagonists & inhibitors*
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gag Gene Products, Human Immunodeficiency Virus / metabolism
Substances
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DNA-Binding Proteins
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Endosomal Sorting Complexes Required for Transport
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Peptides, Cyclic
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Transcription Factors
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Tsg101 protein
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Vesicular Transport Proteins
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gag Gene Products, Human Immunodeficiency Virus
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p6 gag protein, Human immunodeficiency virus 1