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Article

Comparative Analysis of Hepatitis C Virus NS5A Dynamics and Localization in Assembly-Deficient Mutants

1
University of Lille, CNRS, Inserm, Institut Pasteur de Lille, CHU Lille, U1019-UMR 8204-CIIL-Center for Infection and Immunity of Lille, 59000 Lille, France
2
University of Lille, CNRS, UMR 8576-UGSF-Department of Functional and Structural Glycobiology, 59000 Lille, France
3
University of Lille, CNRS, Inserm, Institut Pasteur de Lille, CHU Lille, US 41-UMS 2014-PLBS, 59000 Lille, France
4
Institute of Biochemistry of the Romanian Academy, 060031 Bucharest, Romania
*
Author to whom correspondence should be addressed.
Present address: Calibr, a Division of The Scripps Research Institute, 11119 North Torrey Pines Road, La Jolla, CA 92037, USA.
Academic Editors: Nicola Coppola and Che Colpitts
Pathogens 2021, 10(2), 172; https://doi.org/10.3390/pathogens10020172
Received: 15 December 2020 / Revised: 26 January 2021 / Accepted: 30 January 2021 / Published: 4 February 2021
(This article belongs to the Special Issue Hepatitis C Virus: Remaining Challenges)
The hepatitis C virus (HCV) life cycle is a tightly regulated process, during which structural and non-structural proteins cooperate. However, the interplay between HCV proteins during genomic RNA replication and progeny virion assembly is not completely understood. Here, we studied the dynamics and intracellular localization of non-structural 5A protein (NS5A), which is a protein involved both in genome replication and encapsidation. An NS5A-eGFP (enhanced green fluorescent protein) tagged version of the strain JFH-1-derived wild-type HCV was compared to the corresponding assembly-deficient viruses Δcore, NS5A basic cluster 352–533 mutant (BCM), and serine cluster 451 + 454 + 457 mutant (SC). These analyses highlighted an increase of NS5A motility when the viral protein core was lacking. Although to a lesser extent, NS5A motility was also increased in the BCM virus, which is characterized by a lack of interaction of NS5A with the viral RNA, impairing HCV genome encapsidation. This observation suggests that the more static NS5A population is mainly involved in viral assembly rather than in RNA replication. Finally, NS4B exhibited a reduced co-localization with NS5A and lipid droplets for both Δcore and SC mutants, which is characterized by the absence of interaction of NS5A with core. This observation strongly suggests that NS5A is involved in targeting NS4B to lipid droplets (LDs). In summary, this work contributes to a better understanding of the interplay between HCV proteins during the viral life cycle. View Full-Text
Keywords: hepatitis C virus; NS5A dynamics; NS4B; core; lipid droplets; assembly hepatitis C virus; NS5A dynamics; NS4B; core; lipid droplets; assembly
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MDPI and ACS Style

Riva, L.; Spriet, C.; Barois, N.; Popescu, C.-I.; Dubuisson, J.; Rouillé, Y. Comparative Analysis of Hepatitis C Virus NS5A Dynamics and Localization in Assembly-Deficient Mutants. Pathogens 2021, 10, 172. https://doi.org/10.3390/pathogens10020172

AMA Style

Riva L, Spriet C, Barois N, Popescu C-I, Dubuisson J, Rouillé Y. Comparative Analysis of Hepatitis C Virus NS5A Dynamics and Localization in Assembly-Deficient Mutants. Pathogens. 2021; 10(2):172. https://doi.org/10.3390/pathogens10020172

Chicago/Turabian Style

Riva, Laura, Corentin Spriet, Nicolas Barois, Costin-Ioan Popescu, Jean Dubuisson, and Yves Rouillé. 2021. "Comparative Analysis of Hepatitis C Virus NS5A Dynamics and Localization in Assembly-Deficient Mutants" Pathogens 10, no. 2: 172. https://doi.org/10.3390/pathogens10020172

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