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Volume 73, Issue 12

Carbohydrate determinant NeuAc-Gal(1-4) of -linked glycans modulates the antigenic activity of human immunodeficiency virus type 1 glycoprotein gp120 Free

Abstract

In the present study we investigated to what extent the peripheral carbohydrate structure of -linked glycans influences the antigenic properties of human immunodeficiency virus type 1 glycoprotein 120 (gp120). Recombinant gp120 was purified from GMK cells infected with a recombinant vaccinia virus expressing gp120. Purified gp120 was then coated onto 96-well ELISA microplates and subjected to sequential removal of peripheral monosaccharide units. Modified or unmodified gp120 was then incubated with monoclonal antibodies recognizing specific epitopes of gp120 and with a reporter lectin to determine the extent of carbohydrate elimination. Antibody and lectin binding was quantified in an enzyme-linked system. We found that the carbohydrate structure NeuAc-Galβ(1-4) of -linked glycans, defined both by lectin reactivity and by specific glycosidases, is involved in modulating the binding of antibody to a number of epitopes of peptide nature. The binding of antibody to one class of epitopes, situated in a region between amino acids 200 and 230, was strongly increased by removal of NeuAc-Galβ(1-4). whereas the binding to epitopes in the V3 region was decreased and the binding to epitopes in the far -terminal region was not altered by the treatment. These results suggested that peripheral structures of -glycans are involved in modulating the overall conformation of gp120.

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© Journal of General Virology 1992
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1992-12-01
2024-05-01
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Carbohydrate determinant NeuAc-Galβ(1-4) of N-linked glycans modulates the antigenic activity of human immunodeficiency virus type 1 glycoprotein gp120
J. Gen. Virol. 73, 3099 (1992); https://doi.org/10.1099/0022-1317-73-12-3099
/content/journal/jgv/10.1099/0022-1317-73-12-3099
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