Visualization and analysis of hepatitis C virus structural proteins at lipid droplets by super-resolution microscopy
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Visualization and analysis of hepatitis C virus structural proteins at lipid droplets by super-resolution microscopy. / Eggert, Dennis; Rösch, Kathrin; Reimer, Rudolph; Herker, Eva.
In: PLOS ONE, Vol. 9, No. 7, 2014, p. e102511.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Visualization and analysis of hepatitis C virus structural proteins at lipid droplets by super-resolution microscopy
AU - Eggert, Dennis
AU - Rösch, Kathrin
AU - Reimer, Rudolph
AU - Herker, Eva
PY - 2014
Y1 - 2014
N2 - 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.
AB - 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.
KW - Hepacivirus/metabolism
KW - Lipid Droplets/ultrastructure
KW - Microscopy, Confocal
KW - Microscopy, Fluorescence/methods
KW - Viral Structural Proteins/chemistry
U2 - 10.1371/journal.pone.0102511
DO - 10.1371/journal.pone.0102511
M3 - SCORING: Journal article
C2 - 25019511
VL - 9
SP - e102511
JO - PLOS ONE
JF - PLOS ONE
SN - 1932-6203
IS - 7
ER -
