Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site

@article{Dey2009StructureBasedSO,
  title={Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site},
  author={Barna Dey and Krisha Svehla and Ling Xu and Dianne Wycuff and Tongqing Zhou and G. S. Voss and Adhuna Phogat and Bimal K. Chakrabarti and Yuxing Li and George D Shaw and Peter D. Kwong and Gary J. Nabel and John R. Mascola and Richard T. Wyatt},
  journal={PLoS Pathogens},
  year={2009},
  volume={5},
  pages={806 - 810}
}
The human immunodeficiency virus type 1 (HIV-1) exterior envelope glycoprotein, gp120, possesses conserved binding sites for interaction with the primary virus receptor, CD4, and also for the co-receptor, generally CCR5. Although gp120 is a major target for virus-specific neutralizing antibodies, the gp120 variable elements and its malleable nature contribute to evasion of effective host-neutralizing antibodies. To understand the conformational character and immunogenicity of the gp120 receptor… CONTINUE READING
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