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Glycobiology vol 4 no 1 pp. 13-21, 1994
© 1994

research-article

Interactions of HIV-1 and HIV-2 envelope glycoproteins with sulphated polysaccharides and mannose-6-phosphate

Elisabeth Mbemba, Jean Claude Gluclman1 and Liliane Gattegno

Laboratoire de Biologic Cellulaire Faculté Médecine Paris-Nord, 93012 Bobigny
1CNRS URA 1463, CERVI, Faculté de Médecine and Hôpital Pitié-Salpëtrière 75651 Paris Cedex 13, France

Received on April 5, 1993; revised on October 14, 1993; accepted on October 15, 1993

Envelope glycoproteins of human immunodeficiency viruses (HIV-1 and HIV-2) can interact with high-mannose glycans and with the mannosyl or N-acetylglucosaminyl core of complex-type oligosaccharidic structures. HIV-1 glycoproteins also specifically bind sulphated polysaccharides such as dextran sulphate (DS) and heparin. Here, we show that the latter property is shared by HIV-2 recombinant gp140 (rgpl40) precursor glycoprotein. Binding of rgpl40 and of corresponding rgp160 of HIV-1 to heparin- and DS-substituted (sulphated dextran beads; SDB) affinity matrices was inhibited by the soluble specific ligand and also by fetuin, asialofetuin or the anionic simple carbohydrate derivative manncsse-6-phosphate (M6P). Interaction of HIV-1 rgpl20 subunit with the two affinity matrices was also inhibited by M6P, but only rgpl20 binding to heparin-agarose, and not that to SDB, was affected by fetuin and asialofetuin. These results suggest that HIV-1 and HIV-2 envelope glycoproteins presumably display different sulphated polysaccharide and carbohydrate recognition sites. Some of these may be common or in close proximity: with respect to rgpl60, for example, the sites may be common on the gp41 moiety and/or in a region of gp120 which would be more accessible when expressed on rgpl60 than on processed gpl20, while they may be distinct on the cleaved gpl20 subunit. Finally, because M6P is a marker of lysosomal enzymes, we verified that HIV-1 and HIV-2 envelope glycoproteins could specifically bind in a M6P-inhibitable manner to a representative lysosomal enzyme, bovine liver ß-glucuronidase coupled to agarose, suggesting that they may possibly interfere with lysosomal enzyme sorting in HIV-infected cells.

env glycoproteins HIV lectin mannose-6-phosphate sulphated polysaccharides


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E. Mbemba, J. C. Gluckman, and L. Gattegno
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[Abstract] [Full Text] [PDF]


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