Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions. Academic Article uri icon

Overview

MeSH

  • Antibodies, Neutralizing
  • Antigens, CD4
  • Fluorescence Resonance Energy Transfer
  • Humans
  • Ligands
  • Models, Chemical
  • Molecular Imaging
  • Protein Multimerization
  • Protein Structure, Tertiary

MeSH Major

  • HIV Envelope Protein gp120
  • HIV-1
  • Immune Evasion
  • Virion

abstract

  • The HIV-1 envelope (Env) mediates viral entry into host cells. To enable the direct imaging of conformational dynamics within Env, we introduced fluorophores into variable regions of the glycoprotein gp120 subunit and measured single-molecule fluorescence resonance energy transfer within the context of native trimers on the surface of HIV-1 virions. Our observations revealed unliganded HIV-1 Env to be intrinsically dynamic, transitioning between three distinct prefusion conformations, whose relative occupancies were remodeled by receptor CD4 and antibody binding. The distinct properties of neutralization-sensitive and neutralization-resistant HIV-1 isolates support a dynamics-based mechanism of immune evasion and ligand recognition. Copyright © 2014, American Association for the Advancement of Science.

publication date

  • November 7, 2014

has subject area

  • Antibodies, Neutralizing
  • Antigens, CD4
  • Fluorescence Resonance Energy Transfer
  • HIV Envelope Protein gp120
  • HIV-1
  • Humans
  • Immune Evasion
  • Ligands
  • Models, Chemical
  • Molecular Imaging
  • Protein Multimerization
  • Protein Structure, Tertiary
  • Virion

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC4304640

Digital Object Identifier (DOI)

  • 10.1126/science.1254426

PubMed ID

  • 25298114

Additional Document Info

start page

  • 759

end page

  • 763

volume

  • 346

number

  • 6210