Hepatitis C virus infection and tight junction proteins: The ties that bind.
Claudin-1
Hepatitis C virus
Occludin
Tight junctions
Viral entry and spreading
Journal
Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713
Informations de publication
Date de publication:
01 07 2020
01 07 2020
Historique:
received:
13
01
2020
revised:
25
03
2020
accepted:
28
03
2020
pubmed:
9
4
2020
medline:
24
10
2020
entrez:
9
4
2020
Statut:
ppublish
Résumé
The hepatitis C virus (HCV) is a major cause of liver diseases ranging from liver inflammation to advanced liver diseases like cirrhosis and hepatocellular carcinoma (HCC). HCV infection is restricted to the liver, and more specifically to hepatocytes, which represent around 80% of liver cells. The mechanism of HCV entry in human hepatocytes has been extensively investigated since the discovery of the virus 30 years ago. The entry mechanism is a multi-step process relying on several host factors including heparan sulfate proteoglycan (HSPG), low density lipoprotein receptor (LDLR), tetraspanin CD81, Scavenger Receptor class B type I (SR-BI), Epidermal Growth Factor Receptor (EGFR) and Niemann-Pick C1-like 1 (NPC1L1). Moreover, in order to establish a persistent infection, HCV entry is dependent on the presence of tight junction (TJ) proteins Claudin-1 (CLDN1) and Occludin (OCLN). In the liver, tight junction proteins play a role in architecture and homeostasis including sealing the apical pole of adjacent cells to form bile canaliculi and separating the basolateral domain drained by sinusoidal blood flow. In this review, we will highlight the role of liver tight junction proteins in HCV infection, and we will discuss the potential targeted therapeutic approaches to improve virus eradication.
Identifiants
pubmed: 32268133
pii: S0005-2736(20)30127-9
doi: 10.1016/j.bbamem.2020.183296
pmc: PMC7613427
mid: EMS151256
pii:
doi:
Substances chimiques
LDLR protein, human
0
Membrane Transport Proteins
0
NPC1L1 protein, human
0
OCLN protein, human
0
Occludin
0
Receptors, LDL
0
Tetraspanin 28
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
183296Subventions
Organisme : NIAID NIH HHS
ID : U19 AI123862
Pays : United States
Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest Inserm, the University of Strasbourg and the Strasbourg University Hospitals have filed patent applications for the use of anti-Claudin1 antibodies for treatment of HCV infection which have been licensed to Alentis Therapeutics, Basel, Switzerland.
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