The extracellular processing of HIV‐1 envelope glycoprotein gp160 by human plasmin

FEBS Letters

Towatari, Takae¹  Kido, Hiroshi¹  Okumura, Yuushi¹  Yano, Mihiro¹  Mori, Sachie¹  Murakami, Meiko¹ 

[1] Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima 770, Japan

关键词: Plasmin;    gp160;    Processing;    Human immunodeficiency virus;    HIV-1;    human immunodeficiency virus type 1;    VEM;    viral envelope glycoprotein maturase;    AIDS;    acquired immune deficiency syndrome;    dec;    decanoyl;    cmk;    chloromethyl ketone;    mAb;    monoclonal antibody;    Boc;    N-tert-butyloxycarbonyl;    MCA;    4-methylcoumaryl-7-amide;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    uPA;    urokinase-type plasminogen activator;    PBS;    phosphate-buffered saline;    BSA;    bovine serum albumin;    FCS;    fetal calf serum;    FITC;    fluorescein isothiocyanate;   

DOI  :  10.1016/S0014-5793(98)01612-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown