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J Biol Chem. 2010 Jul 2;285(27):20860-9. doi: 10.1074/jbc.M109.085472. Epub 2010 May 3.

Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.

Author information

  • 1Department of Immunology, Palacky University in Olomouc, Olomouc 77100, Czech Republic. raskamil@uab.edu

Abstract

Human immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design.

PMID:
20439465
[PubMed - indexed for MEDLINE]
PMCID:
PMC2898351
Free PMC Article
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