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