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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Okumura Y,Yano M,Murakami M,Mori S,Towatari T,Kido Hdoi
10.1016/s0014-5793(98)01612-3subject
Has Abstractpub_date
1999-01-08 00:00:00pages
39-42issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01612-3journal_volume
442pub_type
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