n-acetyl-beta-d-glucosaminyl-binding properties of the envelope glycoprotein of human immunodeficiency virus type 1.

NLM AIDSLINE N-Acetyl-beta-D-glucosaminyl-binding properties of the envelope glycoprotein of human immunodeficiency virus type 1. Gattegno L; Sadeghi H; Saffar L; Bladier D; Clerget-Raslain B; Gluckman
February 28, 1992

Carbohydr Res. 1991 Jun 25;213:79-93. Unique Identifier : AIDSLINE The effect of carbohydrate structures on the adsorption of HIV-1 or of recombinant envelope glycoprotein gp 160 (rgp 160) to cells of the CEM line was investigated with an indirect immunofluorescence assay using gp 120-specific mouse monoclonal antibodies (mAbs) directed to envelope gp 120. The beta-D-galactosyl, alpha-D-mannosyl, beta-D-glucosyl, N-acetyl-beta-D-glucosaminyl, sialosyl, and L-fucosyl derivatives tested had no effect on this binding. However, preincubation of HIV-1 (or rgp 160) with the neoglycoprotein, beta-D-GlcNAc47-BSA, specifically inhibited the labeling, by some of the mAb used, of HIV-1 (or rgp 160) bound at the cell membrane. This inhibition occurred only with mAbs that were specific for the immunodominant neutralizing third variable region (V3) of gp 120. Competition for the binding to rgp 160 between beta-D-GlcNAc47-BSA and mAb was further demonstrated by use of affinity matrices substituted with one of the relevant mAb (110-4), or with beta-D-GlcNAc47-BSA. Besides beta-D-GlcNAc47-BSA-Sepharose, rgp 160 also bound with low affinity, but high specificity, to two other N-acetyl-beta-D-glucosaminyl affinity matrices, beta-D-GlcNAc-divinylsulfone-agarose and asialoagalactothyroglobulin-agarose. Conversely, beta-D-[125I]GlcNAc47-BSA bound specifically to gp 160-Sepharose. These results indicated that rgp 160 behaves as a N-acetyl-beta-D-glucosaminyl-binding protein for GlcNAc residues presented at high density on a carrier, the carbohydrate-binding site of which is close to, or located on the V3 region of gp 120. Acetylglucosamine/METABOLISM Antibodies, Monoclonal/METABOLISM Binding Sites Binding, Competitive Carbohydrates/METABOLISM Cell Line Cell Membrane/METABOLISM CD4-Positive T-Lymphocytes/METABOLISM Gene Products, env/METABOLISM Human HIV Antibodies/METABOLISM HIV-1/METABOLISM Lectins/METABOLISM Protein Precursors/METABOLISM Receptors, HIV/METABOLISM Serum Albumin, Bovine/METABOLISM Support, Non-U.S. Gov't JOURNAL ARTICLE

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Information in this article was accurate in February 28, 1992. The state of the art may have changed since the publication date. This material is designed to support, not replace, the relationship that exists between you and your doctor. Always discuss treatment options with a doctor who specializes in treating HIV.