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Detection of orientation‐specific anti‐gp120 antibodies by a new N‐glycanase protection assay

Several functions have been assigned to the extensive glycosylation of HIV‐1 envelope glycoprotein gp120, especially immune escape mechanisms, but the intramolecular interactions between gp120 and its carbohydrate complement are not well understood. To analyse this phenomenon we established a new microwell deglycosylation assay for determining N‐linked glycan accessibility after binding of gp120‐specific agents. Orientation‐specific exposition of gp120 in ELISA microplates was achieved by catching with either anti‐C5 antibody D7324 or anti‐V3 antibody NEA‐9205. We found that soluble CD4 inhibited the deglycosylation of gp120 only when gp120 was caught by D7324 and not by NEA9205. In contrast, antibodies from HIV‐infected individuals inhibited the deglycosylation best when gp120 was caught by NEA9205. These results demonstrated that both the CD4‐binding site and the epitopes recognised by antibodies from HIV‐infected individuals have N‐glycans in the close vicinity. However, the difference in gp120 orientation indicates that antibodies in HIV‐infected individuals, at least partly, bind to epitopes different from the CD4‐binding site.