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

Academic Article


  • 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 immunerecognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed anewapproach to characterize cellspecific 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.
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    Digital Object Identifier (doi)

    Author List

  • Raska M; Takahashi K; Czernekova L; Zachova K; Hall S; Moldoveanu Z; Elliott MC; Wilson L; Brown R; Jancova D
  • Start Page

  • 20860
  • End Page

  • 20869
  • Volume

  • 285
  • Issue

  • 27