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The role of calcium andN-linked glycans in the oligomerization and carbohydrate binding properties of human immunodeficiency virus external envelope glycoprotein

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Abstract

Envelope glycoproteins of human immunodeficiency virus (gp120 and gp41) occur as oligomers. Here, we show by gel filtration analysis that gp 120 oligomerizationin vitro is calcium- and temperature-dependent. Recombinant gp120 (rgp120) species were recovered as monomers at 20 °C in the absence of calcium, but as tetramers at 37 °C in 10mm CaCl2. Under the latter condition,N-glycanase-deglycosylated rgp120 formed hexamers. Relative to intact rgp120, which has been reported to display carbohydrate-binding properties forN-acetyl-β-d-glucosaminyl and mannosyl residues, deglycosylation enhanced rgp120 specific binding to mannose-divinylsulfone-agarose, para-aminophenyl-β-d-GlcNAc-agarose and fetuin-agarose matrices. Taken together, these results rule out the role of homologous lectin-carbohydrate interactions viaN-linked glycans in the rgp120 oligomerization, even though its lectin properties may also be calcium-dependent. Deglycosylation may unmask domains of rgp120 polypeptide backbone that independently play a role either in rgp120 lectin activity or in calcium-dependent oligomerization.

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Authors and Affiliations

  1. Laboratoire de Biologie Cellulaire, Faculté de Médecine Paris-Nord, 93012, Bobigny, France

    Mhenia Haidar & Liliane Gattegno

  2. CNRS URA 1463, CERVI, Hôpital de la Pitié-Salpêtrière, 75651, Paris Cedex 13, France

    Nabila Seddiki & Jean Claude Gluckman

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  1. Mhenia Haidar
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  2. Nabila Seddiki
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  3. Jean Claude Gluckman
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  4. Liliane Gattegno
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Haidar, M., Seddiki, N., Gluckman, J.C. et al. The role of calcium andN-linked glycans in the oligomerization and carbohydrate binding properties of human immunodeficiency virus external envelope glycoprotein. Glycoconjugate J 11, 73–79 (1994). https://doi.org/10.1007/BF00731146

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  • DOI: https://doi.org/10.1007/BF00731146

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