Structure-based vaccine design in HIV: blind men and the elephant?

Curr Pharm Des. 2010;16(33):3744-53. doi: 10.2174/138161210794079173.

Abstract

Traditional vaccine approaches have failed for HIV and novel strategies are now being sought to develop immunogens designed to elicit specific activity against known broad neutralization epitopes. Structure-based vaccine design has great potential but, thus far, remains a largely unproven concept. Further structural information for the envelope (Env) glycoproteins, gp120 and gp41, is needed, particularly for understanding trimer-specific antibodies and their epitopes and to clarify atomic details of the structural elements responsible for masking crucial epitopes and for mediating the conformational rearrangements undertaken during the process of receptor-binding and membrane fusion.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • AIDS Vaccines / immunology*
  • Animals
  • Antibodies, Neutralizing / immunology
  • Drug Design*
  • Epitopes / chemistry
  • Epitopes / immunology
  • HIV Envelope Protein gp120 / chemistry
  • HIV Envelope Protein gp120 / immunology
  • HIV Envelope Protein gp41 / chemistry
  • HIV Envelope Protein gp41 / immunology
  • HIV Infections / prevention & control*
  • HIV-1 / immunology*
  • HIV-1 / metabolism
  • Humans
  • Peptide Fragments / chemistry
  • Peptide Fragments / immunology
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Vaccines, Synthetic / chemistry
  • Vaccines, Synthetic / immunology
  • env Gene Products, Human Immunodeficiency Virus / chemistry*
  • env Gene Products, Human Immunodeficiency Virus / immunology*

Substances

  • AIDS Vaccines
  • Antibodies, Neutralizing
  • Epitopes
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41
  • Peptide Fragments
  • Vaccines, Synthetic
  • env Gene Products, Human Immunodeficiency Virus