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Quantitative super-resolution imaging reveals protein stoichiometry and nanoscale morphology of assembling HIV-Gag virions.

Authors
  • Gunzenhäuser, Julia
  • Olivier, Nicolas
  • Pengo, Thomas
  • Manley, Suliana
Type
Published Article
Journal
Nano Letters
Publisher
American Chemical Society
Publication Date
Sep 12, 2012
Volume
12
Issue
9
Pages
4705–4710
Identifiers
DOI: 10.1021/nl3021076
PMID: 22906128
Source
Medline
License
Unknown

Abstract

The HIV structural protein Gag assembles to form spherical particles of radius ∼70 nm. During the assembly process, the number of Gag proteins increases over several orders of magnitude from a few at nucleation to thousands at completion. The challenge in studying protein assembly lies in the fact that current methods such as standard fluorescence or electron microscopy techniques cannot access all stages of the assembly process in a cellular context. Here, we demonstrate an approach using super-resolution fluorescence imaging that permits quantitative morphological and molecular counting analysis over a wide range of protein cluster sizes. We applied this technique to the analysis of hundreds of HIV-Gag clusters at the cellular plasma membrane, thus elucidating how different fluorescent labels can change the assembly of virions.

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