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

Document type :

Article dans une revue scientifique

DOI :

10.1111/tra.12680

PMID :

31328852

Title :

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

Author(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]

Journal title :

Traffic

Pages :

753-773

Publisher :

Wiley

Publication date :

2019-08-11

ISSN :

1398-9219

English keyword(s) :

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

HAL domain(s) :

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

English abstract : [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 ...
Show more >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.Show less >

Language :

Anglais

Peer reviewed article :

Oui

Audience :

Internationale

Popular science :

Non

Collections :

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

Source :

Harvested from HAL

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