کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5590546 | 1570149 | 2017 | 45 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The unexpected function of a highly conserved YXXΦ motif in HCV core protein
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کلمات کلیدی
ITAMsCCVsPFVHCV coreTGNPrototype foamy virusLDSVZVPBSMUTORFAPs - AP هاMAPK - MAPKMutant - جهش یافتهimmunoreceptor tyrosine-based activation motifs - روندهای فعال سازی مبتنی بر ایمونورسپتور تیروزینTrans-Golgi network - شبکه Trans-Goljiendoplasmic reticulum - شبکه آندوپلاسمی phosphate buffer saline - فسفات بافر شورopen reading frame - قاب خواندن بازLipid droplets - قطرات لیپیدElectron microscopy - میکروسکوپ الکترونیwild type - نوع وحشیReplication - همانندسازی Varicella-zoster virus - ویروس واریسلا-زوسترAdaptor proteins - پروتئین آداپتورclathrin-coated vesicles - کیسه های کلاچری پوشش داده شدهmitogen-activated protein kinases - کیناز پروتئین فعال Mitogen
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
بوم شناسی، تکامل، رفتار و سامانه شناسی
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چکیده انگلیسی
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 ΥΧΧΦ 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 YXXΦ motif of HCV core protein is crucial for the architectural integrity of the particulate form of HCVne. Moreover, we show that the YXXΦ 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Infection, Genetics and Evolution - Volume 54, October 2017, Pages 251-262
Journal: Infection, Genetics and Evolution - Volume 54, October 2017, Pages 251-262
نویسندگان
Eirini Karamichali, Elisavet Serti, Aikaterini Gianneli, Aikaterini Papaefthymiou, Athanassios Kakkanas, Pelagia Foka, Alexandros Seremetakis, Konstantina Katsarou, Ioannis P. Trougakos, Urania Georgopoulou,