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Article ; Online: [Anti-hepatitis C Virus Strategy Targeting the Entry Steps].

Fukasawa, Masayoshi

Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan

2018 Volume 139, Issue 1, Page(s) 89–95

Abstract: Hepatitis C virus (HCV) infection is a major leading cause of chronic severe liver diseases such as cirrhosis and hepatocellular carcinoma. The recent direct-acting antivirals (DAAs) for the treatment of HCV infection offer very high cure rates, but DAAs ...

Abstract	Hepatitis C virus (HCV) infection is a major leading cause of chronic severe liver diseases such as cirrhosis and hepatocellular carcinoma. The recent direct-acting antivirals (DAAs) for the treatment of HCV infection offer very high cure rates, but DAAs are vulnerable to drug resistance because HCV is an RNA virus, which generally has very high mutation rates. DAA resistance-associated variants of HCV could reduce the effectiveness of DAAs in the future. Thus, the continuous development of new anti-HCV drugs against different target molecules is needed. We have been studying the host factors involved in HCV entry into cells. From those studies, we obtained novel candidates for host-targeting anti-HCV entry inhibitors, such as monoclonal antibodies against HCV receptors, which can be used together with DAAs. In this symposium review, we present and discuss our recent work on anti-HCV strategies targeting HCV entry steps.
MeSH term(s)	Animals ; Antibodies, Monoclonal/pharmacology ; Antibodies, Monoclonal/therapeutic use ; Antiviral Agents ; Claudin-1/antagonists & inhibitors ; Drug Discovery ; Drug Resistance, Viral ; Hepacivirus/drug effects ; Hepacivirus/pathogenicity ; Hepatitis C/drug therapy ; Hepatitis C/virology ; Humans ; Mice ; Molecular Targeted Therapy ; Occludin/antagonists & inhibitors ; Receptors, Virus/immunology
Chemical Substances	Antibodies, Monoclonal ; Antiviral Agents ; Claudin-1 ; Occludin ; Receptors, Virus
Language	Japanese
Publishing date	2018-12-31
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	200514-1
ISSN	1347-5231 ; 0031-6903 ; 0372-7750 ; 0919-2085 ; 0919-2131
ISSN (online)	1347-5231
ISSN	0031-6903 ; 0372-7750 ; 0919-2085 ; 0919-2131
DOI	10.1248/yakushi.18-00164-5
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Article: Hazara orthonairovirus nucleoprotein facilitates viral cell-to-cell spread by modulating tight junction protein, claudin-1.

Ohta, Keisuke / Saka, Naoki / Fukasawa, Masayoshi / Nishio, Machiko

Frontiers in microbiology

2023 Volume 14, Page(s) 1192956

Abstract: Background: Tight junctions act as a barrier that prevents invasion of pathogens through epithelial cells. This study aims to elucidate the correlation between tight junctions and nairoviruses using Hazara orthonairovirus (HAZV) as a surrogate model for ...

Abstract	Background: Tight junctions act as a barrier that prevents invasion of pathogens through epithelial cells. This study aims to elucidate the correlation between tight junctions and nairoviruses using Hazara orthonairovirus (HAZV) as a surrogate model for Crimean-Congo hemorrhagic fever virus. Methods: mRNA, total protein, and cell surface protein levels of tight junction proteins were examined by quantitative real-time reverse transcription polymerase chain reaction, immunoblot and flow cytometry, respectively. HAZV growth was measured by plaque assay. Immunofluorescence assay was used to examine viral cell-to-cell spread. The interaction between HAZV nucleoprotein and claudin-1 was analyzed by immunoprecipitation. Results: HAZV infection induced mRNA of several tight junction proteins, especially claudin-1. HAZV infection also induced cell surface expression of claudin-1 protein. Claudin-1 overexpression inhibited the growth of HAZV by blocking its cell-to-cell spread. In contrast, HAZV nucleoprotein completely inhibited HAZV-induced cell surface expression of claudin-1, and this inhibition required interaction between HAZV nucleoprotein and claudin-1. Conclusion: HAZV nucleoprotein was shown to bind to claudin-1 to negatively regulate its cell surface expression, and so can promote cell-to-cell spread of HAZV. This is the first presentation of a possible mechanism behind how nairoviruses counteract tight junction barrier function.
Language	English
Publishing date	2023-05-23
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2023.1192956
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Article: Anti-hepatitis C virus strategy targeting host entry factor claudin-1.

Fukasawa, Masayoshi

Uirusu

2015 Volume 65, Issue 2, Page(s) 245–254

Abstract: Chronic hepatitis C virus (HCV) infection is a major threat to global public health, because it is significantly correlated with the development of severe liver diseases including cirrhosis and hepatocellular carcinomas. Host molecules as well as viral ... ...

Abstract	Chronic hepatitis C virus (HCV) infection is a major threat to global public health, because it is significantly correlated with the development of severe liver diseases including cirrhosis and hepatocellular carcinomas. Host molecules as well as viral factors are promising targets for anti-HCV preventive and therapeutic strategies. Multiple host factors such as CD81, SRBI, claudin-1, and occludin are involved in HCV entry into hepatocytes. In this paper, I first introduce our anti-HCV strategy targeting for host tight junction protein claudin-1. And this review also summarizes developments of other entry inhibitors to prevent initiation of HCV infection and spread. Entry inhibitors might be useful in blocking primary infections, such those as after liver transplantation, and in combination therapies with other anti-HCV agents such as direct-acting antivirals.
MeSH term(s)	Animals ; Antibodies, Monoclonal/therapeutic use ; Antiviral Agents/therapeutic use ; Claudin-1/immunology ; Claudin-1/physiology ; Drug Discovery ; Hepacivirus/growth & development ; Hepacivirus/pathogenicity ; Hepatitis C, Chronic/drug therapy ; Hepatitis C, Chronic/prevention & control ; Hepatitis C, Chronic/virology ; Humans ; Life Cycle Stages/genetics ; Liver/virology ; Mice ; Molecular Targeted Therapy ; Virus Replication/genetics
Chemical Substances	Antibodies, Monoclonal ; Antiviral Agents ; Claudin-1
Language	Japanese
Publishing date	2015
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	603272-2
ISSN	0042-6857
ISSN	0042-6857
DOI	10.2222/jsv.65.245
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Article ; Online: [Claudin 1 as a target for anti-hepatitis C virus strategy].

Fukasawa, Masayoshi

Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan

2014 Volume 134, Issue 5, Page(s) 635–640

Abstract: Chronic hepatitis C virus (HCV) infection is a global public health issue because ～30% of HCV-carriers develop severe liver diseases including hepatic steatosis, cirrhosis, and hepatocellular carcinoma. Not only viral factors but also host/viral ... ...

Abstract	Chronic hepatitis C virus (HCV) infection is a global public health issue because ～30% of HCV-carriers develop severe liver diseases including hepatic steatosis, cirrhosis, and hepatocellular carcinoma. Not only viral factors but also host/viral interactions are promising targets for antiviral preventive and therapeutic strategies. Recent studies showed that a tight junction protein claudin 1 is involved in HCV entry into host cells. Consistent with these studies, we isolated the several hepatic Huh7-derived cell clones defective in claudin 1 as HCV-resistant mutants, and cellular permissiveness to HCV was restored by expression of claudin 1 into these cell mutants. These results strongly suggest that claudin 1 is a promising target for antiviral therapy. We thus tried to isolate antibodies against extracellular domain of human claudin 1. Finally we established four mouse anti-claudin 1 monoclonal antibodies by using DNA immunization method and hybridoma screening with the above claudin 1-defective mutant. In the cell culture-infection system using Huh7.5.1 cells and HCV-JFH1 strain, these four antibodies efficiently inhibited infection by HCV in a dose-dependent manner, but do not affect tight junction localization of claudin 1 and cellular barrier function. These monoclonal antibodies targeting claudin 1 might be useful for preventing HCV infection, such as after liver transplantation, and also blocking viral spread in HCV-infected patients.
MeSH term(s)	Animals ; Antibodies, Monoclonal/immunology ; Claudin-1/immunology ; Hepacivirus/immunology ; Humans ; Liver/immunology ; Tetraspanin 28/immunology ; Tight Junctions/immunology
Chemical Substances	Antibodies, Monoclonal ; Claudin-1 ; Tetraspanin 28
Language	Japanese
Publishing date	2014-04-25
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	200514-1
ISSN	1347-5231 ; 0031-6903 ; 0372-7750 ; 0919-2085 ; 0919-2131
ISSN (online)	1347-5231
ISSN	0031-6903 ; 0372-7750 ; 0919-2085 ; 0919-2131
DOI	10.1248/yakushi.14-00006-4
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Article ; Online: Several catechins and flavonols from green tea inhibit severe fever with thrombocytopenia syndrome virus infection in vitro.

Ogawa, Motohiko / Shimojima, Masayuki / Saijo, Masayuki / Fukasawa, Masayoshi

Journal of infection and chemotherapy : official journal of the Japan Society of Chemotherapy

2020 Volume 27, Issue 1, Page(s) 32–39

Abstract: Introduction: Severe fever with thrombocytopenia syndrome (SFTS) is an emerging tick-borne hemorrhagic fever caused by SFTS virus (SFTSV). The mortality rate of SFTS is pretty high, but no vaccines and antiviral drugs are currently available.: Methods! ...

Abstract	Introduction: Severe fever with thrombocytopenia syndrome (SFTS) is an emerging tick-borne hemorrhagic fever caused by SFTS virus (SFTSV). The mortality rate of SFTS is pretty high, but no vaccines and antiviral drugs are currently available. Methods: The antiviral effects of six green tea-related polyphenols, including four catechins and two flavonols, on SFTSV were evaluated to identify natural antiviral compounds. Results: Pretreatment with all polyphenols inhibited SFTSV infection in a concentration-dependent manner. The half-maximal inhibitory concentrations of (-)-epigallocatechin gallate (EGCg) and (-)-epigallocatechin (EGC) were 1.7-1.9 and 11-39 μM, respectively. The selectivity indices of EGCg and EGC were larger than those of the other polyphenols. Furthermore, pretreatment with EGCg and EGC dose-dependently decreased viral attachment to the host cells. Additionally, the treatment of infected cells with EGCg and EGC inhibited infection more significantly at a lower multiplicity of infection (MOI) than at a higher MOI, and this effect was less effective than that of pretreatment. Pyrogallol, a trihydroxybenzene that is the structural backbone of both EGCg and EGC, also inhibited SFTSV infection, as did gallic acid. Conclusions: Our study revealed that green tea-related polyphenols, especially EGCg and EGC, are useful as candidate anti-SFTSV drugs. Furthermore, the structural basis of their antiviral activity was identified, which should enable investigations of more active drugs in the future.
MeSH term(s)	Catechin/pharmacology ; Flavonols ; Hemorrhagic Fevers, Viral ; Humans ; Severe Fever with Thrombocytopenia Syndrome ; Tea
Chemical Substances	Flavonols ; Tea ; Catechin (8R1V1STN48)
Language	English
Publishing date	2020-08-28
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1355399-9
ISSN	1437-7780 ; 1341-321X
ISSN (online)	1437-7780
ISSN	1341-321X
DOI	10.1016/j.jiac.2020.08.005
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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: The combination of levodopa with levodopa-metabolizing enzyme inhibitors prevents severe fever with thrombocytopenia syndrome virus infection in vitro more effectively than single levodopa.

Ogawa, Motohiko / Murae, Mana / Mizukami, Tomoharu / Gemba, Ryutaro / Irie, Takuya / Shimojima, Masayuki / Ebihara, Hideki / Noguchi, Kohji / Fukasawa, Masayoshi

Journal of infection and chemotherapy : official journal of the Japan Society of Chemotherapy

2023 Volume 29, Issue 5, Page(s) 549–553

Abstract: Severe fever with thrombocytopenia syndrome is a hemorrhagic fever caused by a tick-borne infection. The causative agent, Dabie bandavirus, is also called the severe fever with thrombocytopenia syndrome virus (SFTSV). Ogawa et al. (2022) reported that ... ...

Abstract	Severe fever with thrombocytopenia syndrome is a hemorrhagic fever caused by a tick-borne infection. The causative agent, Dabie bandavirus, is also called the severe fever with thrombocytopenia syndrome virus (SFTSV). Ogawa et al. (2022) reported that levodopa, an antiparkinsonian drug with an o-dihydroxybenzene backbone, which is important for anti-SFTSV activity, inhibited SFTSV infection. Levodopa is metabolized by dopa decarboxylase (DDC) and catechol-O-methyltransferase (COMT) in vivo. We evaluated the anti-SFTSV efficacy of two DDC inhibitors, benserazide hydrochloride and carbidopa, and two COMT inhibitors, entacapone and nitecapone, which also have an o-dihydroxybenzene backbone. Only DDC inhibitors inhibited SFTSV infection with pretreatment of the virus (half-maximal inhibitory concentration [IC
MeSH term(s)	Humans ; Levodopa/pharmacology ; Levodopa/therapeutic use ; Carbidopa ; Catechol O-Methyltransferase/metabolism ; Severe Fever with Thrombocytopenia Syndrome/drug therapy ; Catechols/pharmacology ; Catechols/therapeutic use ; Enzyme Inhibitors/therapeutic use ; Phlebovirus
Chemical Substances	Levodopa (46627O600J) ; entacapone (4975G9NM6T) ; Carbidopa (MNX7R8C5VO) ; Catechol O-Methyltransferase (EC 2.1.1.6) ; Catechols ; Enzyme Inhibitors
Language	English
Publishing date	2023-03-03
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1355399-9
ISSN	1437-7780 ; 1341-321X
ISSN (online)	1437-7780
ISSN	1341-321X
DOI	10.1016/j.jiac.2023.02.017
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Article ; Online: Cellular lipid droplets and hepatitis C virus life cycle.

Fukasawa, Masayoshi

Biological & pharmaceutical bulletin

2009 Volume 33, Issue 3, Page(s) 355–359

Abstract: Lipid droplets (LDs) are cellular lipid storage organelles involved not only in lipid homeostasis but also in a variety of diseases. Chronic hepatitis C virus (HCV) infection affects host lipid metabolism, and thus induces LD accumulation in the liver. ... ...

Abstract	Lipid droplets (LDs) are cellular lipid storage organelles involved not only in lipid homeostasis but also in a variety of diseases. Chronic hepatitis C virus (HCV) infection affects host lipid metabolism, and thus induces LD accumulation in the liver. Recent studies have suggested that cellular LDs also play a crucial role in the HCV life cycle. Interactions between HCV proteins, especially the core protein, and LDs are required for the morphogenesis of infectious HCV. The present minireview will summarize the recent research progress about this unique relationship between LDs and the HCV life cycle.
MeSH term(s)	Hepacivirus/physiology ; Hepatitis C/metabolism ; Hepatitis C/virology ; Host-Pathogen Interactions ; Humans ; Lipid Metabolism ; Lipids ; Organelles/metabolism ; Viral Proteins/metabolism
Chemical Substances	Lipids ; Viral Proteins
Language	English
Publishing date	2009-10-07
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1150271-x
ISSN	1347-5215 ; 0918-6158
ISSN (online)	1347-5215
ISSN	0918-6158
DOI	10.1248/bpb.33.355
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Article ; Online: Overcoming antibody-resistant SARS-CoV-2 variants with bispecific antibodies constructed using non-neutralizing antibodies.

Inoue, Tetsuya / Yamamoto, Yuichiro / Sato, Kaoru / Okemoto-Nakamura, Yuko / Shimizu, Yoshimi / Ogawa, Motohiko / Onodera, Taishi / Takahashi, Yoshimasa / Wakita, Takaji / Kaneko, Mika K / Fukasawa, Masayoshi / Kato, Yukinari / Noguchi, Kohji

iScience

2024 Volume 27, Issue 4, Page(s) 109363

Abstract: A current challenge is the emergence of SARS-CoV-2 variants, such as BQ.1.1 and XBB.1.5, that can evade immune defenses, thereby limiting antibody drug effectiveness. Emergency-use antibody drugs, including the widely effective bebtelovimab, are losing ... ...

Abstract	A current challenge is the emergence of SARS-CoV-2 variants, such as BQ.1.1 and XBB.1.5, that can evade immune defenses, thereby limiting antibody drug effectiveness. Emergency-use antibody drugs, including the widely effective bebtelovimab, are losing their benefits. One potential approach to address this issue are bispecific antibodies which combine the targeting abilities of two antibodies with distinct epitopes. We engineered neutralizing bispecific antibodies in the IgG-scFv format from two initially non-neutralizing antibodies, CvMab-6 (which binds to the receptor-binding domain [RBD]) and CvMab-62 (targeting a spike protein S2 subunit epitope adjacent to the known anti-S2 antibody epitope). Furthermore, we created a bispecific antibody by incorporating the scFv of bebtelovimab with our anti-S2 antibody, demonstrating significant restoration of effectiveness against bebtelovimab-resistant BQ.1.1 variants. This study highlights the potential of neutralizing bispecific antibodies, which combine existing less effective anti-RBD antibodies with anti-S2 antibodies, to revive the effectiveness of antibody therapeutics compromised by immune-evading variants.
Language	English
Publishing date	2024-02-29
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2024.109363
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Article: Establishment of Vero cell lines persistently harboring a yellow fever virus 17D subgenomic replicon

Saito, Kyoko / Shimasaki, Kentaro / Fukasawa, Masayoshi / Suzuki, Ryosuke / Okemoto-Nakamura, Yuko / Katoh, Kaoru / Takasaki, Tomohiko / Hanada, Kentaro

Virus research. 2022 Sept. 20,

2022

Abstract: Yellow fever virus (YFV), a member of the genus Flavivirus, family Flaviviridae, is the etiological agent for an acute viral hemorrhagic disease, yellow fever. Although effective live attenuated vaccines based on the strain YFV 17D are currently ... ...

Abstract	Yellow fever virus (YFV), a member of the genus Flavivirus, family Flaviviridae, is the etiological agent for an acute viral hemorrhagic disease, yellow fever. Although effective live attenuated vaccines based on the strain YFV 17D are currently available, no specific antiviral drug is available, and the disease remains a major public health concern. Hence, the discovery and development of antiviral drugs should lead to great benefits in controlling the disease. To provide a screening platform for antiviral agents targeting YFV RNA translation/replication, we have established and characterized two Vero cell lines that persistently harbor a subgenomic replicon derived from YFV 17D-204 (referred to as replicon cells). The replicon carries YFV nucleotides (1−176 and 2,382−10,862) and a green fluorescent protein (GFP)-Zeocin resistance fusion gene as a selection marker and indicator of persistent replication. Immunofluorescence analysis revealed that both replicon cells and YFV 17D-infected cells showed similar distribution patterns of viral NS4B protein and replication intermediate, double-stranded RNA. Sequencing analysis of persistent replicons from the two replicon cell lines suggested that their nucleotide sequences did not vary greatly following multiple passages. We examined the effect of five agents, the antiviral cytokines interferon-β and -γ, the nucleoside analog ribavirin, the squalene synthase inhibitor zaragozic acid A, and the antibiotic rifapentine, a recently reported entry and replication inhibitor against YFV, on the persistent replication in the two replicon cell lines. These agents were selected because they inhibited both production of YFV 17D and transient replication of a luciferase-expressing replicon in Vero cells, without greatly affecting cell viability. We found that each of the agents decreased GFP fluorescence in the replicon cells, albeit to varying degrees. The agents other than rifapentine also showed a decrease in viral RNA levels in the replicon cells comparable to that seen for GFP fluorescence. These results indicate that persistent replication is susceptible to each of these five agents, although their mechanisms of action may differ. Taken together, these results provide evidence that translation/replication of the replicon in the replicon cells mimics that of the viral genome upon YFV 17D infection, indicating that the replicon cell lines can serve as a useful tool for high-throughput antiviral drug screening.
Keywords	Yellow fever virus ; antibiotics ; antiviral agents ; cell viability ; cytokines ; double-stranded RNA ; etiological agents ; fluorescence ; fluorescent antibody technique ; genes ; green fluorescent protein ; live vaccines ; nucleosides ; nucleotides ; public health ; replicon ; research ; squalene ; viral genome ; viruses ; yellow fever
Language	English
Dates of publication	2022-0920
Publishing place	Elsevier B.V.
Document type	Article
Note	Pre-press version
ZDB-ID	605780-9
ISSN	1872-7492 ; 0168-1702
ISSN (online)	1872-7492
ISSN	0168-1702
DOI	10.1016/j.virusres.2022.198935
Database	NAL-Catalogue (AGRICOLA)

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