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J. Biol. Chem., Vol. 265, Issue 15, 8519-8524, 05, 1990
T Mizuochi, TJ Matthews, M Kato, J Hamako, K Titani, J Solomon and T Feizi
The N-linked oligosaccharide structures on the envelope glycoprotein gp120
of human immunodeficiency virus 1 derived from chronically infected
lymphoblastoid (H9) cells have been investigated by enzymatic
microsequencing after release from protein by hydrazinolysis, labeling with
NaB3H4, and chromatography on adsorbent columns of Phaseolus vulgaris
erythrophytohemagglutinin and Ricinus communis agglutinin (Mr 120,000) and
on Bio-Gel P-4. A substantially greater diversity of oligosaccharide
structures was detected than among those released by hydrazinolysis from
recombinant gp120 produced in Chinese hamster ovary cells and investigated
by similar procedures (Mizuochi, T., Spellman, M.W., Larkin, M., Solomon,
J., Basa, L.J., and Feizi, T. (1988) Biochem J. 254, 599-603) and among
those released by endoglycosidases from virus-derived gp120 isolated from
infected H9 cells after metabolic labeling with D-[2-3H]mannose or
D-[6-3H]glucosamine (Geyer, H., Holschbach, L., Hunsmann, G., and
Schneider, J. (1988) J. Biol. Chem. 263, 11760-11767). In this study, 16%
of the oligosaccharides were identified as complex-type bi-, tri-, and
tetraantennary sialo- oligosaccharides with bisecting N-acetylglucosamine
residues. Such structures were lacking on recombinant gp120 and could not
be detected on the metabolically labeled, virus-derived glycoprotein. As in
the earlier investigations, complex-type chains lacking bisecting N-
acetylglucosamine residues, hybrid-type chains, and a series of high
mannose-type structures with 5-9 mannose residues were identified. In
addition, an array of complex-type chains having one or more outer chains
with beta-galactosyl residues were detected in this study, but with
additional substitutions that require further investigation. The number of
potential N-glycosylation sites on gp120 is on the order of 20, but the
oligosaccharide structures are far more numerous. Thus, the salient
conclusion from this and earlier investigations is that alternative
structures occur on at least some of the glycosylation sites and that
numerous glycosylation variants of this glycoprotein are produced even
within a single cell line. Since the glycosylation is the product of host
cell glycosyltransferases, an even greater number of glycosylation variants
of gp120 are predicted to arise from the heterogeneous cell populations
harboring the virus in in vivo infection.
Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N- acetylglucosamine residues
Division of Biomedical Polymer Science, Fujita Health University, Aichi, Japan.
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