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Article: Roles of the two distinct proteasome pathways in hepatitis C virus infection.

Shoji, Ikuo

2013 Volume 1, Issue 2, Page(s) 44–50

Abstract: Hepatitis C virus (HCV) infection often causes chronic hepatitis, liver cirrhosis, and hepatocellular carcinoma. The development of a HCV cell culture system enabled us to investigate its whole HCV life cycle and develop a better understanding of the ... ...

Abstract	Hepatitis C virus (HCV) infection often causes chronic hepatitis, liver cirrhosis, and hepatocellular carcinoma. The development of a HCV cell culture system enabled us to investigate its whole HCV life cycle and develop a better understanding of the pathogenesis of this virus. Post-translational modification plays a crucial role in HCV replication and in the maturation of viral particles. There is growing evidence also suggesting that the ubiquitin-proteasome pathway and the ubiquitin-independent proteasome pathway are involved in the stability control of HCV proteins. Many viruses are known to manipulate the proteasome pathways to modulate the cell cycle, inhibit apoptosis, evade the immune system, and activate cell signaling, thereby contributing to persistent infection and viral carcinogenesis. The identification of functional interactions between HCV and the proteasome pathways will therefore shed new light on the life cycle and pathogenesis of HCV. This review summarizes the current knowledge on the involvement of the ubiquitin-dependent and -independent proteasome pathways in HCV infection and discusses the roles of these two distinct mechanisms in HCV pathogenesis.
Language	English
Publishing date	2013-07-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2829019-7
ISSN	2220-3249
ISSN	2220-3249
DOI	10.5501/wjv.v1.i2.44
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Article ; Online: Transcription Factor JunB Suppresses Hepatitis C Virus Replication.

Ariffianto, Adi / Deng, Lin / Harada, Saki / Liang, Yujiao / Matsui, Chieko / Abe, Takayuki / Shoji, Ikuo

The Kobe journal of medical sciences

2023 Volume 69, Issue 3, Page(s) E86–E95

Abstract: We previously reported that hepatitis C virus (HCV) infection activates the reactive oxygen species (ROS)/c-Jun N-terminal kinase (JNK) signaling pathway. Activation of JNK contributes to the development of liver diseases, including metabolic disorders, ... ...

Abstract	We previously reported that hepatitis C virus (HCV) infection activates the reactive oxygen species (ROS)/c-Jun N-terminal kinase (JNK) signaling pathway. Activation of JNK contributes to the development of liver diseases, including metabolic disorders, steatosis, liver cirrhosis and hepatocellular carcinoma. JNK is known to have numerous target genes, including JunB, a member of activator protein-1 transcription factor family. However, the roles of JunB in the HCV life cycle and HCV-associated pathogenesis remain unclear. To clarify a physiological role of JunB in HCV infection, we investigated the phosphorylation of JunB in HCV J6/JFH1-infected Huh-7.5 cells. Immunoblot analysis revealed that HCV-induced ROS/JNK activation promoted phosphorylation of JunB. The small interfering RNA (siRNA) knockdown of JunB significantly increased the amount of intracellular HCV RNA as well as the intracellular and extracellular HCV infectivity titers. Conversely, overexpression of JunB significantly reduced the amount of intracellular HCV RNA and the intracellular and extracellular HCV infectivity titers. These results suggest that JunB plays a role in inhibiting HCV propagation. Additionally, HCV-mediated JunB activation promoted hepcidin promoter activity and hepcidin mRNA levels, a key factor in modulating iron homeostasis, suggesting that JunB is involved in HCV-induced transcriptional upregulation of hepcidin. Taken together, we propose that the HCV-induced ROS/JNK/JunB signaling pathway plays roles in inhibiting HCV replication and contributing to HCV-mediated iron metabolism disorder.
MeSH term(s)	Humans ; Hepacivirus ; Hepcidins ; Reactive Oxygen Species ; Hepatitis C ; Transcription Factors ; RNA ; Liver Neoplasms ; Virus Replication
Chemical Substances	Hepcidins ; Reactive Oxygen Species ; Transcription Factors ; RNA (63231-63-0) ; JunB protein, human
Language	English
Publishing date	2023-08-31
Publishing country	Japan
Document type	Journal Article
ZDB-ID	840671-6
ISSN	1883-0498 ; 0023-2513
ISSN (online)	1883-0498
ISSN	0023-2513
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Zs.A 193: Show issues

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Article ; Online: The Role of Chaperone-Mediated Autophagy in Hepatitis C Virus-Induced Pathogenesis.

Matsui, Chieko / Yuliandari, Putu / Deng, Lin / Abe, Takayuki / Shoji, Ikuo

Frontiers in cellular and infection microbiology

2021 Volume 11, Page(s) 796664

Abstract: Lysosome incorporate and degrade proteins in a process known as autophagy. There are three types of autophagy; macroautophagy, microautophagy, and chaperone-mediated autophagy (CMA). Although autophagy is considered a nonselective degradation process, ... ...

Abstract	Lysosome incorporate and degrade proteins in a process known as autophagy. There are three types of autophagy; macroautophagy, microautophagy, and chaperone-mediated autophagy (CMA). Although autophagy is considered a nonselective degradation process, CMA is known as a selective degradation pathway. All proteins internalized in the lysosome
MeSH term(s)	Autophagy ; Chaperone-Mediated Autophagy ; Hepacivirus ; Hepatitis C ; Humans ; Lysosomal-Associated Membrane Protein 2 ; Lysosomes ; Molecular Chaperones
Chemical Substances	Lysosomal-Associated Membrane Protein 2 ; Molecular Chaperones
Language	English
Publishing date	2021-12-02
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2021.796664
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Article ; Online: Hepatitis C Virus Disrupts Annexin 5-Mediated Occludin Integrity through Downregulation of Protein Kinase Cα (PKCα) and PKCη Expression, Thereby Promoting Viral Propagation.

Abe, Takayuki / Marutani, Yuki / Deng, Lin / Matsui, Chieko / Fukasawa, Masayoshi / Suzuki, Ryosuke / Wakita, Takaji / Matsuura, Yoshiharu / Shoji, Ikuo

Journal of virology

2023 Volume 97, Issue 6, Page(s) e0065523

Abstract: Annexins (ANXs) comprise a family of calcium- and phospholipid-binding proteins and are implicated in the hepatitis C virus (HCV) life cycle. Here, we demonstrate a novel role of ANX5 in the HCV life cycle. Comparative analysis by quantitative PCR in ... ...

Abstract	Annexins (ANXs) comprise a family of calcium- and phospholipid-binding proteins and are implicated in the hepatitis C virus (HCV) life cycle. Here, we demonstrate a novel role of ANX5 in the HCV life cycle. Comparative analysis by quantitative PCR in human hepatoma cells revealed that ANX2, ANX4, and ANX5 were highly expressed among the ANX family proteins. Knockdown of ANX5 mRNA resulted in marked enhancement of HCV RNA replication but had no effect on either HCV translation or assembly. Using the HCV pseudoparticle (HCVpp) system, we observed enhancement of HCVpp infectivity in ANX5 knockdown Huh-7OK1 cells, suggesting that ANX5 is involved in suppression of HCV entry. Additionally, we observed that subcellular localizations of tight-junction proteins, such as claudin 1 (CLDN1) and occludin (OCLN), were disrupted in the ANX5 knockdown cells. It was reported that HCV infection was facilitated by disruption of OCLN distribution and that proper distribution of OCLN was regulated by its phosphorylation. Knockdown of ANX5 resulted in a decrease of OCLN phosphorylation, thereby disrupting OCLN distribution and HCV infection. Further analysis revealed that protein kinase C (PKC) isoforms, including PKCα and PKCη, play important roles in the regulation of ANX5-mediated phosphorylation and distribution of OCLN and in the restriction of HCV infection. HCV infection reduced OCLN phosphorylation through the downregulation of PKCα and PKCη expression. Taken together, these results suggest that ANX5, PKCα, and PKCη contribute to restriction of HCV infection by regulating OCLN integrity. We propose a model that HCV disrupts ANX5-mediated OCLN integrity through downregulation of PKCα and PKCη expression, thereby promoting HCV propagation.
MeSH term(s)	Humans ; Annexin A5/genetics ; Annexin A5/metabolism ; Down-Regulation ; Hepacivirus/physiology ; Hepatitis C ; Occludin/genetics ; Occludin/metabolism ; Protein Isoforms/genetics ; Protein Kinase C-alpha/genetics ; Protein Kinase C-alpha/metabolism ; Virus Internalization
Chemical Substances	Annexin A5 ; Occludin ; OCLN protein, human ; Protein Isoforms ; protein kinase C eta (EC 2.7.1.-) ; Protein Kinase C-alpha (EC 2.7.11.13) ; ANXA5 protein, human
Language	English
Publishing date	2023-06-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.00655-23
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Article ; Online: Cytosolic DNA-sensing immune response and viral infection.

Abe, Takayuki / Marutani, Yuki / Shoji, Ikuo

Microbiology and immunology

2019 Volume 63, Issue 2, Page(s) 51–64

Abstract: How host cells recognize many kinds of RNA and DNA viruses and initiate innate antiviral responses against them has not yet been fully elucidated. Over the past decade, investigations into the mechanisms underlying these antiviral responses have focused ... ...

Abstract	How host cells recognize many kinds of RNA and DNA viruses and initiate innate antiviral responses against them has not yet been fully elucidated. Over the past decade, investigations into the mechanisms underlying these antiviral responses have focused extensively on immune surveillance sensors that recognize virus-derived components (such as lipids, sugars and nucleic acids). The findings of these studies have suggested that antiviral responses are mediated by cytosolic or intracellular compartment sensors and their adaptor molecules (e.g., TLR, myeloid differentiation primary response 88, retinoic acid inducible gene-I, IFN-β promoter stimulator-1, cyclic GMP-AMP synthase and stimulator of IFN genes axis) for the primary sensing of virus-derived nucleic acids, leading to production of type I IFNs, pro-inflammatory cytokines and chemokines by the host cells. Thus, host cells have evolved an elaborate host defense machinery to recognize and eliminate virus infections. In turn, to achieve sustained viral infection and induce pathogenesis, viruses have also evolved several counteracting strategies for achieving immune escape by targeting immune sensors, adaptor molecules, intracellular kinases and transcription factors. In this review, we discuss recent discoveries concerning the role of the cytosolic nucleic acid-sensing immune response in viral recognition and control of viral infection. In addition, we consider the regulatory machinery of the cytosolic nucleic acid-sensing immune response because these immune surveillance systems must be tightly regulated to prevent aberrant immune responses to self and non-self-nucleic acids.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Animals ; Antiviral Agents/immunology ; Chemokines/metabolism ; Cytokines/metabolism ; Cytosol/immunology ; Cytosol/virology ; DNA, Viral/immunology ; DNA, Viral/metabolism ; Host-Pathogen Interactions/immunology ; Humans ; Immune Evasion ; Immunity, Innate ; Interferon-beta/genetics ; Interferons/metabolism ; Myeloid Differentiation Factor 88/genetics ; Myeloid Differentiation Factor 88/metabolism ; Nucleic Acids ; Nucleotidyltransferases/genetics ; Signal Transduction ; Transcription Factors/genetics ; Virus Diseases/immunology ; Viruses/immunology ; Viruses/pathogenicity
Chemical Substances	Adaptor Proteins, Signal Transducing ; Antiviral Agents ; Chemokines ; Cytokines ; DNA, Viral ; MYD88 protein, human ; Myeloid Differentiation Factor 88 ; Nucleic Acids ; Transcription Factors ; Interferon-beta (77238-31-4) ; Interferons (9008-11-1) ; Nucleotidyltransferases (EC 2.7.7.-) ; cGAS protein, human (EC 2.7.7.-)
Keywords	covid19
Language	English
Publishing date	2019-02-26
Publishing country	Australia
Document type	Journal Article ; Review
ZDB-ID	224792-6
ISSN	1348-0421 ; 0385-5600
ISSN (online)	1348-0421
ISSN	0385-5600
DOI	10.1111/1348-0421.12669
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Article ; Online: NS5A-ISGylation via Lysine 26 Has a Critical Role for Efficient Propagation of Hepatitis C Virus Genotype 2a.

Bawono, Rheza Gandi / Abe, Takayuki / Shibata, Yasuaki / Matsui, Chieko / Deng, Lin / Shoji, Ikuo

The Kobe journal of medical sciences

2021 Volume 67, Issue 2, Page(s) E38–E47

Abstract: We previously reported that hepatitis C virus (HCV) NS5A (1b, Con1) protein accepts covalent ISG15 conjugation at specific lysine (Lys) residues (K44, K68, K166, K215 and K308), exhibiting proviral effects on HCV RNA replication. Here we investigated a ... ...

Abstract	We previously reported that hepatitis C virus (HCV) NS5A (1b, Con1) protein accepts covalent ISG15 conjugation at specific lysine (Lys) residues (K44, K68, K166, K215 and K308), exhibiting proviral effects on HCV RNA replication. Here we investigated a role of NS5A-ISGylation via Lys residues in HCV propagation using HCV infectious clone. The alignment of amino acid sequences revealed that 5 Lys residues (K20, K26, K44, K139, and K166) of the 13 Lys residues within NS5A (genotype 2a, JFH1 strain) were conserved compared to those of HCV (genotype 1b, Con1 strain). The cell-based ISGylation assay revealed that the K26 residue in the amphipathic helix (AH) domain and the K139 residue in domain I of NS5A (2a, JFH1) had the potential to accept ISGylation. Use of the HCV replicon carrying luciferase gene revealed that the K26 residue but not K139 residue of NS5A (2a, JFH1) was important for HCV RNA replication. Furthermore, cell culture HCV revealed that the mutation with the K26 residue in combination with K139 or K166 on NS5A (2a, JFH1) resulted in complete abolishment of viral propagation, suggesting that the K26 residue collaborates with either the K139 residue or K166 residue for efficient HCV propagation. Taken together, these results suggest that HCV NS5A protein has the potential to accept ISGylation via specific Lys residues, involving efficient viral propagation in a genotype-specific manner.
MeSH term(s)	Cytokines ; Genotype ; Hepacivirus/genetics ; Hepacivirus/physiology ; Hepatitis C ; Humans ; Lysine ; RNA, Viral ; Ubiquitins ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Virus Replication/genetics
Chemical Substances	Cytokines ; RNA, Viral ; Ubiquitins ; Viral Nonstructural Proteins ; ISG15 protein, human (60267-61-0) ; NS-5 protein, hepatitis C virus (EC 2.7.7.48) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2021-09-30
Publishing country	Japan
Document type	Journal Article
ZDB-ID	840671-6
ISSN	1883-0498 ; 0023-2513
ISSN (online)	1883-0498
ISSN	0023-2513
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Article ; Online: Hepatitis C Virus-Induced ROS/JNK Signaling Pathway Activates the E3 Ubiquitin Ligase Itch to Promote the Release of HCV Particles via Polyubiquitylation of VPS4A.

Deng, Lin / Liang, Yujiao / Ariffianto, Adi / Matsui, Chieko / Abe, Takayuki / Muramatsu, Masamichi / Wakita, Takaji / Maki, Masatoshi / Shibata, Hideki / Shoji, Ikuo

Journal of virology

2022 Volume 96, Issue 6, Page(s) e0181121

Abstract: We previously reported that hepatitis C virus (HCV) infection activates the reactive oxygen species (ROS)/c-Jun N-terminal kinase (JNK) signaling pathway. However, the roles of ROS/JNK activation in the HCV life cycle remain unclear. We sought to ... ...

Abstract	We previously reported that hepatitis C virus (HCV) infection activates the reactive oxygen species (ROS)/c-Jun N-terminal kinase (JNK) signaling pathway. However, the roles of ROS/JNK activation in the HCV life cycle remain unclear. We sought to identify a novel role of the ROS/JNK signaling pathway in the HCV life cycle. Immunoblot analysis revealed that HCV-induced ROS/JNK activation promoted phosphorylation of Itch, a HECT-type E3 ubiquitin ligase, leading to activation of Itch. The small interfering RNA (siRNA) knockdown of Itch significantly reduced the extracellular HCV infectivity titers, HCV RNA, and HCV core protein without affecting intracellular HCV infectivity titers, HCV RNA, and HCV proteins, suggesting that Itch is involved in the release of HCV particles. HCV-mediated JNK/Itch activation specifically promoted polyubiquitylation of an AAA-type ATPase, VPS4A, but not VPS4B, required to form multivesicular bodies. Site-directed mutagenesis revealed that two lysine residues (K23 and K121) on VPS4A were important for VPS4A polyubiquitylation. The siRNA knockdown of VPS4A, but not VPS4B, significantly reduced extracellular HCV infectivity titers. Coimmunoprecipitation analysis revealed that HCV infection specifically enhanced the interaction between CHMP1B, a subunit of endosomal sorting complexes required for transport (ESCRT)-III complex, and VPS4A, but not VPS4B, whereas VPS4A K23R/K121R greatly reduced the interaction with CHMP1B. HCV infection significantly increased ATPase activity of VPS4A, but not VPS4A K23R/K121R or VPS4B, suggesting that HCV-mediated polyubiquitylation of VPS4A contributes to activation of VPS4A. Taken together, we propose that the HCV-induced ROS/JNK/Itch signaling pathway promotes VPS4A polyubiquitylation, leading to enhanced VPS4A-CHMP1B interaction and promotion of VPS4A ATPase activity, thereby promoting the release of HCV particles.
MeSH term(s)	ATPases Associated with Diverse Cellular Activities/metabolism ; Adenosine Triphosphatases/metabolism ; Cell Line ; Endosomal Sorting Complexes Required for Transport/metabolism ; Gene Knockdown Techniques ; Hepacivirus/physiology ; Hepatitis C/physiopathology ; Hepatitis C/virology ; Humans ; MAP Kinase Signaling System ; RNA, Small Interfering/metabolism ; Reactive Oxygen Species/metabolism ; Repressor Proteins/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Vacuolar Proton-Translocating ATPases/metabolism ; Virion
Chemical Substances	Endosomal Sorting Complexes Required for Transport ; RNA, Small Interfering ; Reactive Oxygen Species ; Repressor Proteins ; ITCH protein, human (EC 2.3.2.26) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Adenosine Triphosphatases (EC 3.6.1.-) ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; VPS4A protein, human (EC 3.6.4.6)
Language	English
Publishing date	2022-01-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01811-21
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Zs.A 609: Show issues

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Article ; Online: Role of hepcidin upregulation and proteolytic cleavage of ferroportin 1 in hepatitis C virus-induced iron accumulation.

Ohta, Kazuyoshi / Ito, Masahiko / Chida, Takeshi / Nakashima, Kenji / Sakai, Satoshi / Kanegae, Yumi / Kawasaki, Hideya / Aoshima, Takuya / Takabayashi, Shuji / Takahashi, Hirotaka / Kawata, Kazuhito / Shoji, Ikuo / Sawasaki, Tatsuya / Suda, Takafumi / Suzuki, Tetsuro

PLoS pathogens

2023 Volume 19, Issue 8, Page(s) e1011591

Abstract: Hepatitis C virus (HCV) is a pathogen characterized not only by its persistent infection leading to the development of cirrhosis and hepatocellular carcinoma (HCC), but also by metabolic disorders such as lipid and iron dysregulation. Elevated iron load ... ...

Abstract	Hepatitis C virus (HCV) is a pathogen characterized not only by its persistent infection leading to the development of cirrhosis and hepatocellular carcinoma (HCC), but also by metabolic disorders such as lipid and iron dysregulation. Elevated iron load is commonly observed in the livers of patients with chronic hepatitis C, and hepatic iron overload is a highly profibrogenic and carcinogenic factor that increases the risk of HCC. However, the underlying mechanisms of elevated iron accumulation in HCV-infected livers remain to be fully elucidated. Here, we observed iron accumulation in cells and liver tissues under HCV infection and in mice expressing viral proteins from recombinant adenoviruses. We established two molecular mechanisms that contribute to increased iron load in cells caused by HCV infection. One is the transcriptional induction of hepcidin, the key hormone for modulating iron homeostasis. The transcription factor cAMP-responsive element-binding protein hepatocyte specific (CREBH), which was activated by HCV infection, not only directly recognizes the hepcidin promoter but also induces bone morphogenetic protein 6 (BMP6) expression, resulting in an activated BMP-SMAD pathway that enhances hepcidin promoter activity. The other is post-translational regulation of the iron-exporting membrane protein ferroportin 1 (FPN1), which is cleaved between residues Cys284 and Ala285 in the intracytoplasmic loop region of the central portion mediated by HCV NS3-4A serine protease. We propose that host transcriptional activation triggered by endoplasmic reticulum stress and FPN1 cleavage by viral protease work in concert to impair iron efflux, leading to iron accumulation in HCV-infected cells.
MeSH term(s)	Animals ; Mice ; Carcinoma, Hepatocellular ; Hepacivirus/physiology ; Hepatitis C/metabolism ; Hepcidins/genetics ; Hepcidins/metabolism ; Iron/metabolism ; Liver Neoplasms ; Transcriptional Activation ; Up-Regulation
Chemical Substances	Hepcidins ; Iron (E1UOL152H7) ; metal transporting protein 1 ; HAMP protein, human ; Hamp protein, mouse
Language	English
Publishing date	2023-08-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1011591
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Article ; Online: Oxidative stress sensor Keap1 recognizes HBx protein to activate the Nrf2/ARE signaling pathway, thereby inhibiting hepatitis B virus replication.

Ariffianto, Adi / Deng, Lin / Abe, Takayuki / Matsui, Chieko / Ito, Masahiko / Ryo, Akihide / Aly, Hussein Hassan / Watashi, Koichi / Suzuki, Tetsuro / Mizokami, Masashi / Matsuura, Yoshiharu / Shoji, Ikuo

Journal of virology

2023 Volume 97, Issue 10, Page(s) e0128723

Abstract: Importance: The Kelch-like ECH-associated protein 1 (Keap1)/NF-E2-related factor 2 (Nrf2)/antioxidant response element (ARE) signaling pathway is one of the most important defense mechanisms against oxidative stress. We previously reported that a ... ...

Abstract	Importance: The Kelch-like ECH-associated protein 1 (Keap1)/NF-E2-related factor 2 (Nrf2)/antioxidant response element (ARE) signaling pathway is one of the most important defense mechanisms against oxidative stress. We previously reported that a cellular hydrogen peroxide scavenger protein, peroxiredoxin 1, a target gene of transcription factor Nrf2, acts as a novel HBV X protein (HBx)-interacting protein and negatively regulates hepatitis B virus (HBV) propagation through degradation of HBV RNA. This study further demonstrates that the Nrf2/ARE signaling pathway is activated during HBV infection, eventually leading to the suppression of HBV replication. We provide evidence suggesting that Keap1 interacts with HBx, leading to Nrf2 activation and inhibition of HBV replication via suppression of HBV core promoter activity. This study raises the possibility that activation of the Nrf2/ARE signaling pathway is a potential therapeutic strategy against HBV. Our findings may contribute to an improved understanding of the negative regulation of HBV replication by the antioxidant response.
MeSH term(s)	Humans ; Antioxidant Response Elements ; Hepatitis B/genetics ; Hepatitis B virus/physiology ; Kelch-Like ECH-Associated Protein 1/metabolism ; NF-E2-Related Factor 2/metabolism ; Oxidative Stress ; Signal Transduction ; Virus Replication
Chemical Substances	Kelch-Like ECH-Associated Protein 1 ; NF-E2-Related Factor 2 ; KEAP1 protein, human ; hepatitis B virus X protein
Language	English
Publishing date	2023-10-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01287-23
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Article ; Online: Cellular Release of Infectious Hepatitis C Virus Particles via Endosomal Pathways.

Deng, Lin / Solichin, Muchamad Ridotu / Adyaksa, Dewa Nyoman Murti / Septianastiti, Maria Alethea / Fitri, Rhamadianti Aulia / Suwardan, Gede Ngurah Rsi / Matsui, Chieko / Abe, Takayuki / Shoji, Ikuo

Viruses

2023 Volume 15, Issue 12

Abstract: Hepatitis C virus (HCV) is a positive-sense, single-stranded RNA virus that causes chronic hepatitis, liver cirrhosis and hepatocellular carcinoma. The release of infectious HCV particles from infected hepatocytes is a crucial step in viral dissemination ...

Abstract	Hepatitis C virus (HCV) is a positive-sense, single-stranded RNA virus that causes chronic hepatitis, liver cirrhosis and hepatocellular carcinoma. The release of infectious HCV particles from infected hepatocytes is a crucial step in viral dissemination and disease progression. While the exact mechanisms of HCV particle release remain poorly understood, emerging evidence suggests that HCV utilizes intracellular membrane trafficking and secretory pathways. These pathways include the Golgi secretory pathway and the endosomal trafficking pathways, such as the recycling endosome pathway and the endosomal sorting complex required for transport (ESCRT)-dependent multivesicular bodies (MVBs) pathway. This review provides an overview of recent advances in understanding the release of infectious HCV particles, with a particular focus on the involvement of the host cell factors that participate in HCV particle release. By summarizing the current knowledge in this area, this review aims to contribute to a better understanding of endosomal pathways involved in the extracellular release of HCV particles and the development of novel antiviral strategies.
MeSH term(s)	Humans ; Hepacivirus/metabolism ; Hepatitis A ; Endosomes/metabolism ; Hepatitis C ; Virion/metabolism ; Virus Release ; Endosomal Sorting Complexes Required for Transport/metabolism
Chemical Substances	Endosomal Sorting Complexes Required for Transport
Language	English
Publishing date	2023-12-14
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v15122430
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