@article{mbs:/content/journal/jgv/10.1099/0022-1317-73-12-3099, author = "Bolmstedt, Anders and Olofsson, Sigvard and Sjögren-Jansson, Eva and Jeansson, Stig and Sjöblom, Inger and Åkerblom, Lennart and Hansen, John-Erik S. and Hu, Shiu-Lok", title = "Carbohydrate determinant NeuAc-Galβ(1-4) of N-linked glycans modulates the antigenic activity of human immunodeficiency virus type 1 glycoprotein gp120", journal= "Journal of General Virology", year = "1992", volume = "73", number = "12", pages = "3099-3105", doi = "https://doi.org/10.1099/0022-1317-73-12-3099", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-73-12-3099", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "In the present study we investigated to what extent the peripheral carbohydrate structure of N-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 N-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 N-terminal region was not altered by the treatment. These results suggested that peripheral structures of N-glycans are involved in modulating the overall conformation of gp120.", }