Analysis of the interaction of antibodies with a conserved enzymatically deglycosylated core of the HIV type 1 envelope glycoprotein 120.

@article{Binley1998AnalysisOT,
  title={Analysis of the interaction of antibodies with a conserved enzymatically deglycosylated core of the HIV type 1 envelope glycoprotein 120.},
  author={James M Binley and Richard Wyatt and Elizabeth Desjardins and Peter D. Kwong and Wayne A. Hendrickson and John P. Moore and Joseph Sodroski},
  journal={AIDS research and human retroviruses},
  year={1998},
  volume={14 3},
  pages={191-8}
}
The binding of a panel of monoclonal antibodies to V1, V2, and V3 loop-deleted HIV-1 gp120 was studied by competition analysis. Most of the previously defined relationships between gp120 epitopes were preserved on the variable loop-deleted protein, although interactions between some epitopes were dependent on the presence of the V1, V2, and V3 loops. Enzymatic deglycosylation of the variable loop-deleted protein only minimally altered the binding of most antibodies examined. Thus, a… CONTINUE READING

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