Visualization and analysis of hepatitis C virus structural proteins at lipid droplets by super-resolution microscopy

PLoS One. 2014 Jul 11;9(7):e102511. doi: 10.1371/journal.pone.0102511. eCollection 2014.

Abstract

Cytosolic lipid droplets are central organelles in the Hepatitis C Virus (HCV) life cycle. The viral capsid protein core localizes to lipid droplets and initiates the production of viral particles at lipid droplet-associated ER membranes. Core is thought to encapsidate newly synthesized viral RNA and, through interaction with the two envelope proteins E1 and E2, bud into the ER lumen. Here, we visualized the spatial distribution of HCV structural proteins core and E2 in vicinity of small lipid droplets by three-color 3D super-resolution microscopy. We observed and analyzed small areas of colocalization between the two structural proteins in HCV-infected cells with a diameter of approximately 100 nm that might represent putative viral assembly sites.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hepacivirus / metabolism*
  • Lipid Droplets / ultrastructure
  • Lipid Droplets / virology*
  • Microscopy, Confocal
  • Microscopy, Fluorescence / methods
  • Viral Structural Proteins / chemistry
  • Viral Structural Proteins / metabolism*
  • Viral Structural Proteins / ultrastructure

Substances

  • Viral Structural Proteins

Grants and funding

The Heinrich Pette Institute, Leibniz Institute for Experimental Virology is supported by the Free and Hanseatic City of Hamburg and the Federal Ministry of Health. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.