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The role of calcium and N-linked glycans in the oligomerization and carbohydrate binding properties of human immunodeficiency virus external envelope glycoprotein [published erratum appears in Glycoconj J 1994 Oct;11(5):500]
Haidar M; Seddiki N; Gluckman JC; Gattegno L; Laboratoire de Biologie
April 30, 1995
Glycoconj J. 1994 Apr;11(2):73-9. Unique Identifier : AIDSLINE

Envelope glycoproteins of human immunodeficiency virus (gp120 and gp41) occur as oligomers. Here, we show by gel filtration analysis that gp120 oligomerization in vitro is calcium- and temperature-dependent. Recombinant gp120 (rgp120) species were recovered as monomers at 20 degrees C in the absence of calcium, but as tetramers at 37 degrees C in 10 mM CaCl2. Under the latter condition, N-glycanase-deglycosylated rgp120 formed hexamers. Relative to intact rgp120, which has been reported to display carbohydrate-binding properties for N-acetyl-beta-D-glucosaminyl and mannosyl residues, deglycosylation enhanced rgp120 specific binding to mannose-divinylsulfone-agarose, para-aminophenyl-beta-D-GlcNAc-agarose and fetuin-agarose matrices. Taken together, these results rule out the role of homologous lectin-carbohydrate interactions via N-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.

Calcium/PHARMACOLOGY Chromatography, Gel Comparative Study HIV/*METABOLISM HIV Envelope Protein gp120/*CHEMISTRY/METABOLISM HIV Envelope Protein gp41/*CHEMISTRY/METABOLISM Kinetics Lectins Macromolecular Systems Polysaccharides/*METABOLISM/PHARMACOLOGY Recombinant Proteins/CHEMISTRY/METABOLISM Support, Non-U.S. Gov't Thermodynamics JOURNAL ARTICLE