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Effects of calcium ions on proteolytic processing of HIV‐1 gp160 precursor and on cell fusion
Author(s) -
Moulard Maxime,
Montagnier Luc,
Bahraoui Elmostafa
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80284-x
Subject(s) - syncytium , glycoprotein , gp41 , calcium , cell fusion , metalloproteinase , chemistry , microbiology and biotechnology , protease , cytosol , biochemistry , lipid bilayer fusion , cleavage (geology) , transmembrane protein , biology , cell , enzyme , immunology , membrane , fracture (geology) , epitope , antigen , paleontology , receptor , organic chemistry
Complete activation of human immunodeficiency virus type 1 (HIV‐1) requires the endoproteolytic cleavage by cellular protease of the envelope glycoprotein precursor (gp160) into the external glycoprotein gp120, and the transmembrane glycoprotein gp41. We report here the effect of depletion of cellular calcium ions on maturation of precursor gp160 and its concomitant effect on syncytium formation. We show that the cellular endoprotease activity responsible for gp160 maturation and the capacity for HIV‐1 to induce syncytium formation are calcium‐dependent. In addition, we show that endoproteolytic maturation is a key step in syncytium formation induced by HIV‐1.