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

• Published in: PloS one Vol. 9; no. 7; p. e102511
• Main Authors: Eggert, Dennis, Rösch, Kathrin, Reimer, Rudolph, Herker, Eva
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 11.07.2014; Public Library of Science (PLoS)
• Subjects: Biology and life sciences; Capsid protein; Droplets; Hepacivirus - metabolism; Hepatitis; Hepatitis C; Hepatitis C virus; Infections; Lasers; Life cycle engineering; Life cycles; Lipid Droplets - ultrastructure; Lipid Droplets - virology; Lipids; Membranes; Microscopy; Microscopy, Confocal; Microscopy, Fluorescence - methods; Organelles; Proteins; Research and Analysis Methods; Ribonucleic acid; RNA; Spatial distribution; Structural proteins; Viral infections; Viral Structural Proteins - chemistry; Viral Structural Proteins - metabolism; Viral Structural Proteins - ultrastructure; Virology; Viruses; Germany
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0102511

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.