Abstract
Cleavage of the envelope glycoprotein precursor gp160 of HIV-1 is a prerequisite for the infectivity of HIV-1, and occurs at least in part before gp160 reaches the cell surface. Kexin/subtilisin-related endopeptidases are proposed enzyme candidates for this intracellular processing. In this study, we reveal the possibility that plasminogen binds to the cell surface and part of gp160 escaping intracellular processing is cleaved by plasmin extracellularly. Plasmin cleaves gp160 precisely at the C-terminal arginine residue of gp120, and the processing is effectively inhibited by an analogue peptide of the cleavage motif (RXK/RR) and by plasmin inhibitors.
MeSH terms
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Amino Acid Sequence
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Binding Sites / genetics
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Cell Membrane / metabolism
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Cell Membrane / virology
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Clone Cells
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Fibrinolysin / metabolism*
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HIV Envelope Protein gp120 / genetics
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HIV Envelope Protein gp120 / metabolism
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HIV Envelope Protein gp160 / genetics
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HIV Envelope Protein gp160 / metabolism*
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HIV Envelope Protein gp41 / genetics
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HIV Envelope Protein gp41 / metabolism
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HIV-1 / genetics
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HIV-1 / metabolism*
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HIV-1 / pathogenicity
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Humans
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Molecular Sequence Data
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Protein Processing, Post-Translational
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
Substances
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HIV Envelope Protein gp120
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HIV Envelope Protein gp160
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HIV Envelope Protein gp41
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Recombinant Proteins
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Fibrinolysin