%0 Journal Article
%1 10.1371/journal.ppat.1008554
%A Vieyres, G
%A Reichert, I
%A Carpentier, A
%A Vondran, F W R
%A Pietschmann, T
%D 2020
%I Public Library of Science
%J PLOS Pathog
%K pietschmann
%N 6
%P 1-41
%T The ATGL lipase cooperates with ABHD5 to mobilize lipids for hepatitis C virus assembly
%V 16
%X Author summary The multifaceted role of lipid droplets and their position as the main metabolic hub in the cell makes them a coveted target for intracellular pathogens, be there parasites, bacteria or viruses. Lipid droplets are the main energy reservoir of the cell, and this is often the function hijacked by the pathogens. With its low density, its apolipoprotein coat and its neutral lipid core, the HCV particle resembles host-circulating lipoproteins. Here we report that HCV hijacks the lipid droplet-associated adipose triglyceride lipase (ATGL) for its morphogenesis. Given that ABHD5 and to some extent ATGL also participate in lipoprotein secretion, our results indicate that lipid droplets might serve as a source for the lipids of the atypical HCV lipo-viro-particle. They also imply that viral hijacking of the ABHD5-ATGL host machinery might disturb lipid droplet homeostasis thus contributing to HCV-dependent liver steatosis.