<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Karamichali, Eirini</style></author><author><style face="normal" font="default" size="100%">Serti, Elisavet</style></author><author><style face="normal" font="default" size="100%">Gianneli, Aikaterini</style></author><author><style face="normal" font="default" size="100%">Papaefthymiou, Aikaterini</style></author><author><style face="normal" font="default" size="100%">Kakkanas, Athanassios</style></author><author><style face="normal" font="default" size="100%">Foka, Pelagia</style></author><author><style face="normal" font="default" size="100%">Seremetakis, Alexandros</style></author><author><style face="normal" font="default" size="100%">Katsarou, Konstantina</style></author><author><style face="normal" font="default" size="100%">Trougakos, Ioannis P.</style></author><author><style face="normal" font="default" size="100%">Georgopoulou, Urania</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">{The unexpected function of a highly conserved YXX$\Phi$ motif in HCV core protein}</style></title><secondary-title><style face="normal" font="default" size="100%">Infection, Genetics and Evolution</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">AP-2M1</style></keyword><keyword><style  face="normal" font="default" size="100%">HCV core</style></keyword><keyword><style  face="normal" font="default" size="100%">HCVne</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipid droplets</style></keyword><keyword><style  face="normal" font="default" size="100%">Replication</style></keyword><keyword><style  face="normal" font="default" size="100%">YXX$\Phi$ motif</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">oct</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">https://linkinghub.elsevier.com/retrieve/pii/S1567134817302307</style></url></web-urls></urls><publisher><style face="normal" font="default" size="100%">Elsevier B.V.</style></publisher><volume><style face="normal" font="default" size="100%">54</style></volume><pages><style face="normal" font="default" size="100%">251–262</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Hepatitis C virus (HCV) is an RNA positive strand virus, member of the Flaviviridae family. The HCV viral particle is composed of a capsid containing the genome, surrounded by an endoplasmic reticulum (ER)-derived lipid bilayer where E1 and E2 are assembled as heterodimers. However, different forms of viral particles have been identified in the serum of HCV-infected patients, including non-enveloped particles. Previous reports have demonstrated that HCV non-enveloped capsid-like particles (HCVne) can be generated by HCV core protein sequence. This sequence possesses a highly conserved $\Upsilon$ΧΧ$\Phi$ motif and distal di-leucine motifs that confer primary endocytosis signals, enabling HCVne to enter hepatic cells via clathrin-mediated endocytosis. Although HCV core's primary function is to encapsidate the viral genome, it also interacts with a variety of cellular proteins in order to regulate host cell functions such as gene transcription, lipid metabolism, apoptosis and several signaling pathways. In this report, we demonstrate that the YXX$\Phi$ motif of HCV core protein is crucial for the architectural integrity of the particulate form of HCVne. Moreover, we show that the YXX$\Phi$ motif in the HCV core sequence plays a pivotal role in the signaling events following HCVne clathrin-mediated endocytosis by inducing the AP-2 clathrin adaptor protein, which in turn redirect HCVne trafficking to the lipid droplets (LDs) via the endosomal-lysosomal pathway. HCVne and LDs co-localization affects the HCV life cycle by enhancing viral replication.</style></abstract></record></records></xml>