Role of the cytosolic domain of occludin in trafficking and hepatitis C virus infection

Lavie, Muriel; Linna, Lydia; Moustafa, Rehab; Belouzard, Sandrine; Fukasawa, Masayoshi; Dubuisson, Jean

Type de document :

Article dans une revue scientifique: Article original

DOI :

10.1111/tra.12680

PMID :

31328852

Titre :

Role of the cytosolic domain of occludin in trafficking and hepatitis C virus infection

Auteur(s) :

Lavie, Muriel [Auteur correspondant]

Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Linna, Lydia [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Moustafa, Rehab [Auteur]
National Research Centre - NRC (EGYPT)
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Belouzard, Sandrine [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Fukasawa, Masayoshi [Auteur]
National Institute of Infectious Diseases [Tokyo]
Dubuisson, Jean [Auteur]

Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]

Titre de la revue :

Traffic

Pagination :

753-773

Éditeur :

Wiley

Date de publication :

2019-08-11

ISSN :

1398-9219

Mot(s)-clé(s) en anglais :

hepatitis C virus
occludin
tight junctions
trafficking
virus entry
virus-host interaction

Discipline(s) HAL :

Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Virologie

Résumé en anglais : [en]

The role of the tight-junction (TJ) protein occludin (OCLN) in hepatitis C virus (HCV) entry remains elusive. Here, we investigated the OCLN C-terminal cytosolic domain in HCV infection. We expressed a series of C-terminal ...
Lire la suite >The role of the tight-junction (TJ) protein occludin (OCLN) in hepatitis C virus (HCV) entry remains elusive. Here, we investigated the OCLN C-terminal cytosolic domain in HCV infection. We expressed a series of C-terminal deletion mutants in Huh-7 cells KO for OCLN and characterized their functionality in HCV infection and trafficking. Deleting the OCLN cytosolic domain led to protein instability and intracellular retention. The first 15 residues (OCLN-C15 mutant) of the cytosolic domain were sufficient for OCLN stability, but led to its accumulation in the trans-Golgi network (TGN) due to a deficient cell surface export after synthesis. In contrast, the OCLN-C18 mutant, containing the first 18 residues of the cytosolic domain, was expressed at the cell surface and could mediate HCV infection. Point mutations in the context of C18 showed that I279 and W281 are crucial residues for cell surface expression of OCLN-C18. However, in the context of full-length OCLN, mutation of these residues only partially affected infection and cell surface localization. Importantly, the characterization of OCLN-C18 in human-polarized hepatocytes revealed a defect in its TJ localization without affecting HCV infection. These data suggest that TJ localization of OCLN is not a prerequisite for HCV infection in polarized hepatocytes.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Collections :

Centre d'Infection et d'Immunité de Lille (CIIL) - U1019 - UMR 9017

Source :

Harvested from HAL

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