| Autor: |
Gram GJ; Department of Clinical Virology, University of Göteborg, Sweden., Bolmstedt A, Schønning K, Biller M, Hansen JE, Olofsson S |
| Jazyk: |
angličtina |
| Zdroj: |
APMIS : acta pathologica, microbiologica, et immunologica Scandinavica [APMIS] 2002 Feb; Vol. 110 (2), pp. 123-31. |
| DOI: |
10.1034/j.1600-0463.2002.100202.x |
| Abstrakt: |
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. Finally, we determined the structural class of the glycan of one V1 glycosylation site of prototype HIV-1 LAI gp120, which remained unsolved from previous studies, and found that it belonged to the complex type of glycans. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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