Abstract
The [Tyr5,12,Lys7]-polyphemusin II peptide (T22) inhibits HIV-1 replication in lymphocytes. The mechanism of T22 inhibition of HIV-1 replication may involve T22 competition with HIV-1 for attachment sites on the plasma membrane of targeted cells. Here we find that the T22 peptide binds to the CD4 molecule in affinity columns. We also find that antiserum to CD4 inhibits cell attachment to T22. Further CD4+ transfected cells attach to T22 while their parental cells which do not express CD4 do not attach to T22. These data demonstrate that T22 binds to the CD4 molecule and supports the hypothesis that T22 inhibits HIV-1 replication by binding to the cell surface CD4 molecule and inhibiting uptake of the virus.
MeSH terms
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Amino Acid Sequence
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Antigens, CD / isolation & purification
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Antigens, CD / physiology*
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Antimicrobial Cationic Peptides*
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Antiviral Agents / chemistry
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Antiviral Agents / metabolism*
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Antiviral Agents / pharmacology
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Binding Sites
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Binding, Competitive
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CD4 Antigens / isolation & purification
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CD4 Antigens / physiology*
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Cell Adhesion / drug effects
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Cell Line
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Chromatography, Affinity
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HIV-1 / drug effects
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HIV-1 / physiology*
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HeLa Cells
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Humans
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Kinetics
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Molecular Sequence Data
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Peptides / chemistry
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Peptides / metabolism*
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Peptides / pharmacology
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Protein Conformation
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Virus Replication / drug effects
Substances
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Antigens, CD
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Antimicrobial Cationic Peptides
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Antiviral Agents
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CD4 Antigens
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Peptides
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T22 protein, synthetic