Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: characterization and ligand binding analysis.

@article{Pancera2005SolubleMO,
  title={Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: characterization and ligand binding analysis.},
  author={Marie Pancera and Jacob Lebowitz and A. H. Schoen and Ping Zhu and Ernesto Freire and Peter D. Kwong and Kenneth H. Roux and Joseph Sodroski and Richard Wyatt},
  journal={Journal of virology},
  year={2005},
  volume={79 15},
  pages={9954-69}
}
The human immunodeficiency virus type 1 (HIV-1) exterior envelope glycoprotein, gp120, mediates binding to the viral receptors and, along with the transmembrane glycoprotein gp41, is a major target for neutralizing antibodies. We asked whether replacing the gp41 fusion/trimerization domain with a stable trimerization motif might lead to a more stable gp120 trimer that would be amenable to structural and immunologic analysis. To obtain stable gp120 trimers, a heterologous trimerization motif… CONTINUE READING