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Article ; Online: HCV Assembly and Egress via Modifications in Host Lipid Metabolic Systems.

Shimotohno, Kunitada

Cold Spring Harbor perspectives in medicine

2021 Volume 11, Issue 1

Abstract: Hepatitis C virus (HCV) proliferates by hijacking the host lipid machinery. In vitro replication systems revealed many aspects of the virus life cycle; in particular, viral utilization of host lipid metabolism during HCV proliferation. HCV interacts with ...

Abstract	Hepatitis C virus (HCV) proliferates by hijacking the host lipid machinery. In vitro replication systems revealed many aspects of the virus life cycle; in particular, viral utilization of host lipid metabolism during HCV proliferation. HCV interacts with lipid droplets (LDs) before starting the process of virus capsid formation at the lipid-rich endoplasmic reticulum (ER) membrane compartment. HCV buds into the ER via lipoprotein assembly and secretion. Exchangeable apolipoproteins, represented by apolipoprotein E (apoE), play pivotal roles in enhancing HCV-specific infectivity. HCV virions are likely to interact with other lipoproteins circulating in blood vessels and incorporate apolipoproteins as well as lipids. This review focuses on virus assembly and egress by briefly describing the recent advances in this area.
MeSH term(s)	Apolipoproteins/metabolism ; Hepacivirus/physiology ; Hepatitis C/metabolism ; Hepatitis C/virology ; Humans ; Lipid Metabolism ; Lipoproteins/metabolism ; Virion/metabolism ; Virus Assembly
Chemical Substances	Apolipoproteins ; Lipoproteins
Language	English
Publishing date	2021-01-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	2157-1422
ISSN (online)	2157-1422
DOI	10.1101/cshperspect.a036814
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Ubiquitination of SARS-CoV-2 NSP6 and ORF7a Facilitates NF-κB Activation.

Nishitsuji, Hironori / Iwahori, Satoko / Ohmori, Mariko / Shimotohno, Kunitada / Murata, Takayuki

mBio

2022 Volume 13, Issue 4, Page(s) e0097122

Abstract: Patients with severe coronavirus disease 2019 tend to have high levels of proinflammatory cytokines, which eventually lead to cytokine storm and the development of acute respiratory distress syndrome. However, the detailed molecular mechanisms of ... ...

Abstract	Patients with severe coronavirus disease 2019 tend to have high levels of proinflammatory cytokines, which eventually lead to cytokine storm and the development of acute respiratory distress syndrome. However, the detailed molecular mechanisms of proinflammatory cytokine production remain unknown. Here, we screened severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genes and found that nonstructural protein 6 (NSP6) and open reading frame 7a (ORF7a) activated the NF-κB pathway. NSP6 and ORF7a interacted with transforming growth factor β-activated kinase 1 (TAK1), and knockout (KO) of TAK1 or NF-κB essential modulator (NEMO) abolished NF-κB activation by NSP6 and ORF7a. Interestingly, K61 of NSP6 was conjugated to K63-linked polyubiquitin chains by the E3 ubiquitin ligase tripartite motif-containing 13, and this polyubiquitination of NSP6 appeared crucial for recruitment of NEMO to the NSP6-TAK1 complex and NF-κB activation. On the other hand, ring finger protein 121 (RNF121) was required for the polyubiquitination of ORF7a. Knockdown of RNF121 significantly decreased ORF7a binding of TAK1 and NEMO, resulting in the suppression of NF-κB activation. Taken together, our results provide novel molecular insights into the pathogenesis of SARS-CoV-2 and the host immune response to SARS-CoV-2 infection.
MeSH term(s)	COVID-19 ; Cytokines/metabolism ; Humans ; NF-kappa B/metabolism ; Open Reading Frames ; SARS-CoV-2/genetics ; Ubiquitination
Chemical Substances	Cytokines ; NF-kappa B
Language	English
Publishing date	2022-07-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.00971-22
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Article ; Online: N6-methyladenosine Modification of Hepatitis B Virus RNA in the Coding Region of

Murata, Takayuki / Iwahori, Satoko / Okuno, Yusuke / Nishitsuji, Hironori / Yanagi, Yusuke / Watashi, Koichi / Wakita, Takaji / Kimura, Hiroshi / Shimotohno, Kunitada

International journal of molecular sciences

2023 Volume 24, Issue 3

Abstract: N6-methyladenosine ( ... ...

Abstract	N6-methyladenosine (m
MeSH term(s)	Humans ; Hepatitis B virus/genetics ; Hepatitis B virus/metabolism ; Viral Regulatory and Accessory Proteins/genetics ; Trans-Activators/genetics ; Trans-Activators/metabolism ; Virus Replication/genetics ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Hepatitis B
Chemical Substances	Viral Regulatory and Accessory Proteins ; Trans-Activators ; RNA, Viral
Language	English
Publishing date	2023-01-23
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24032265
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Article ; Online: INSTABILITY OF MESSENGER AND RIBOSOMAL RNA IN A GLUE-PROTEIN MUTANT OF Bombyx mori.

Kamijo, Seiji / Kawaguchi, Yutaka / Fujii, Hiroshi / Sakaguchi, Bungo / Doira, Hiroshi / Kuhara, Satoru / Aso, Yoichi / Koga, Katsumi / Hayashi, Katsuya / Shimotohno, Kunitada

Development, growth & differentiation

2023 Volume 20, Issue 4, Page(s) 283–289

Abstract: The mucous glands of Bombyx pupae secrete glue proteins which attach deposited eggs to the mounting sheet. A mutant of a dominant gene, named no glue (Ng), produces nonadhesive eggs which have a low capacity for glue-protein synthesis. In the present ... ...

Abstract	The mucous glands of Bombyx pupae secrete glue proteins which attach deposited eggs to the mounting sheet. A mutant of a dominant gene, named no glue (Ng), produces nonadhesive eggs which have a low capacity for glue-protein synthesis. In the present study it was shown that the mucous glands of Ng silkworms showed rapid degradation of mRNA as well as rRNA during development; this may cause the low capacity for glue-protein synthesis in the mutant organ. In contrast, the mucous glands of normal silkworms showed a significant increase in content of RNA's until the maximum rate of glue-protein synthesis was achieved. The degradation of RNA in the Ng mucous gland was inhibited by actinomycin D injected into the body fluid. Thus it is supposed that the Ng gene codes for a presumptive controller RNA, which would be the mediator of RNA instability in the mucous glands of Ng pupae.
Language	English
Publishing date	2023-06-06
Publishing country	Japan
Document type	Journal Article
ZDB-ID	280433-5
ISSN	1440-169X ; 0012-1592
ISSN (online)	1440-169X
ISSN	0012-1592
DOI	10.1111/j.1440-169X.1978.00283.x
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Zs.A 194: Show issues

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Article ; Online: Antiviral effect of peptoids on hepatitis B virus infection in cell culture.

Murayama, Asako / Igarashi, Hitomi / Yamada, Norie / Aly, Hussein Hassan / Molchanova, Natalia / Lin, Jennifer S / Nishitsuji, Hironori / Shimotohno, Kunitada / Muramatsu, Masamichi / Barron, Annelise E / Kato, Takanobu

Antiviral research

2024 Volume 223, Page(s) 105821

Abstract: Although antimicrobial peptides have been shown to inactivate viruses through disruption of their viral envelopes, clinical use of such peptides has been hampered by a number of factors, especially their enzymatically unstable structures. To overcome the ...

Abstract	Although antimicrobial peptides have been shown to inactivate viruses through disruption of their viral envelopes, clinical use of such peptides has been hampered by a number of factors, especially their enzymatically unstable structures. To overcome the shortcomings of antimicrobial peptides, peptoids (sequence-specific N-substituted glycine oligomers) mimicking antimicrobial peptides have been developed. We aimed to demonstrate the antiviral effects of antimicrobial peptoids against hepatitis B virus (HBV) in cell culture. The anti-HBV activity of antimicrobial peptoids was screened and evaluated in an infection system involving the HBV reporter virus and HepG2.2.15-derived HBV. By screening with the HBV reporter virus infection system, three (TM1, TM4, and TM19) of 12 peptoids were identified as reducing the infectivity of HBV, though they did not alter the production levels of HBs antigen in cell culture. These peptoids were not cytotoxic at the evaluated concentrations. Among these peptoids, TM19 was confirmed to reduce HBV infection most potently in a HepG2.2.15-derived HBV infection system that closely demonstrates authentic HBV infection. In cell culture, the most effective administration of TM19 was virus treatment at the infection step, but the reduction in HBV infectivity by pre-treatment or post-treatment of cells with TM19 was minimal. The disrupting effect of TM19 targeting infectious viral particles was clarified in iodixanol density gradient analysis. In conclusion, the peptoid TM19 was identified as a potent inhibitor of HBV. This peptoid prevents HBV infection by disrupting viral particles and is a candidate for a new class of anti-HBV reagents.
MeSH term(s)	Humans ; Hepatitis B virus ; Peptoids/pharmacology ; Peptoids/chemistry ; Hepatitis B/drug therapy ; Cell Culture Techniques ; Anti-Infective Agents ; Antiviral Agents/pharmacology ; Antimicrobial Peptides
Chemical Substances	Peptoids ; Anti-Infective Agents ; Antiviral Agents ; Antimicrobial Peptides
Language	English
Publishing date	2024-01-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	306628-9
ISSN	1872-9096 ; 0166-3542
ISSN (online)	1872-9096
ISSN	0166-3542
DOI	10.1016/j.antiviral.2024.105821
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Zs.A 1627: Show issues

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Article: Angiotensin–Converting Enzyme (ACE) 1 Gene Polymorphism and Phenotypic Expression of COVID-19 Symptoms

Yamamoto, Naoki / Nishida, Nao / Yamamoto, Rain / Gojobori, Takashi / Shimotohno, Kunitada / Mizokami, Masashi / Ariumi, Yasuo

Genes. 2021 Oct. 01, v. 12, no. 10

2021

Abstract: The renin–angiotensin–aldosterone system (RAAS) appears to play an important role in SARS-CoV-2 infection. Polymorphisms within the genes that control this enzymatic system are candidates for elucidating the pathogenesis of COVID-19, since COVID-19 is ... ...

Abstract	The renin–angiotensin–aldosterone system (RAAS) appears to play an important role in SARS-CoV-2 infection. Polymorphisms within the genes that control this enzymatic system are candidates for elucidating the pathogenesis of COVID-19, since COVID-19 is not only a pulmonary disease but also affects many organs and systems throughout the body in multiple ways. Most striking is the fact that ACE2, one of the major components of the RAAS, is a prerequisite for SARS-COV-2 infection. Recently, we and other groups reported an association between a polymorphism of the ACE1 gene (a homolog of ACE2) and the phenotypic expression of COVID-19, particularly in its severity. The ethnic difference in ACE1 insertion (I)/deletion (D) polymorphism seems to explain the apparent difference in mortality between the West and East Asia. The purpose of this review was to further evaluate the evidence linking ACE1 polymorphisms to COVID-19. We searched the Medline database (2019–2021) for reference citations of relevant articles and selected studies on the clinical outcome of COVID-19 related to ACE1 I/D polymorphism. Although the numbers of patients are not large enough yet, most available evidence supports the notion that the DD genotype adversely influences COVID-19 symptoms. Surprisingly, small studies conducted in several countries yielded opposite results, suggesting that the ACE1 II genotype is a risk factor. This contradictory result may be the case in certain geographic areas, especially in subgroups of patients. It may also be due to interactions with other genes or to yet unexplained biochemical mechanisms. According to our hypothesis, such candidates are genes that are functionally involved in the pathophysiology of COVID-19, can act in concert with the ACE1 DD genotype, and that show differences in their frequency between the West and East Asia. For this, we conducted research focusing on Alu-related genes. The current study on the ACE1 genotype will provide potentially new clues to the pathogenesis, treatment, and diagnosis of SARS-CoV-2 infections.
Keywords	COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; databases ; genes ; genetic polymorphism ; genotype ; mortality ; pathogenesis ; pathophysiology ; peptidyl-dipeptidase A ; phenotype ; respiratory tract diseases ; risk factors ; East Asia
Language	English
Dates of publication	2021-1001
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2527218-4
ISSN	2073-4425
ISSN	2073-4425
DOI	10.3390/genes12101572
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Angiotensin-Converting Enzyme (ACE) 1

Yamamoto, Naoki / Nishida, Nao / Yamamoto, Rain / Gojobori, Takashi / Shimotohno, Kunitada / Mizokami, Masashi / Ariumi, Yasuo

Genes

2021 Volume 12, Issue 10

Abstract: The renin-angiotensin-aldosterone system (RAAS) appears to play an important role in SARS-CoV-2 infection. Polymorphisms within the genes that control this enzymatic system are candidates for elucidating the pathogenesis of COVID-19, since COVID-19 is ... ...

Abstract	The renin-angiotensin-aldosterone system (RAAS) appears to play an important role in SARS-CoV-2 infection. Polymorphisms within the genes that control this enzymatic system are candidates for elucidating the pathogenesis of COVID-19, since COVID-19 is not only a pulmonary disease but also affects many organs and systems throughout the body in multiple ways. Most striking is the fact that ACE2, one of the major components of the RAAS, is a prerequisite for SARS-COV-2 infection. Recently, we and other groups reported an association between a polymorphism of the
MeSH term(s)	COVID-19/genetics ; COVID-19/metabolism ; Gene Expression Regulation, Viral ; Genotype ; Humans ; INDEL Mutation ; Peptidyl-Dipeptidase A/genetics ; Peptidyl-Dipeptidase A/metabolism ; Polymorphism, Genetic ; Risk Factors ; SARS-CoV-2/metabolism
Chemical Substances	ACE protein, human (EC 3.4.15.1) ; Peptidyl-Dipeptidase A (EC 3.4.15.1)
Language	English
Publishing date	2021-10-01
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2527218-4
ISSN	2073-4425 ; 2073-4425
ISSN (online)	2073-4425
ISSN	2073-4425
DOI	10.3390/genes12101572
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Article ; Online: Does Genetic Predisposition Contribute to the Exacerbation of COVID-19 Symptoms in Individuals with Comorbidities and Explain the Huge Mortality Disparity between the East and the West?

Yamamoto, Naoki / Yamamoto, Rain / Ariumi, Yasuo / Mizokami, Masashi / Shimotohno, Kunitada / Yoshikura, Hiroshi

International journal of molecular sciences

2021 Volume 22, Issue 9

Abstract: The elderly and patients with several comorbidities experience more severe cases of coronavirus disease 2019 (COVID-19) than healthy patients without underlying medical conditions. However, it is unclear why these people are prone to developing alveolar ... ...

Abstract	The elderly and patients with several comorbidities experience more severe cases of coronavirus disease 2019 (COVID-19) than healthy patients without underlying medical conditions. However, it is unclear why these people are prone to developing alveolar pneumonia, rapid exacerbations, and death. Therefore, we hypothesized that people with comorbidities may have a genetic predisposition that makes them more vulnerable to various factors; for example, they are likely to become more severely ill when infected with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). To test this hypothesis, we searched the literature extensively. Polymorphisms of genes, such as those that encode angiotensin-converting enzyme 1 (
MeSH term(s)	Aged ; Alleles ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/metabolism ; Animals ; COVID-19/genetics ; COVID-19/metabolism ; COVID-19/physiopathology ; COVID-19/virology ; Comorbidity ; Genetic Predisposition to Disease ; HLA Antigens/genetics ; HLA Antigens/metabolism ; Haplotypes ; Humans ; Inflammation/genetics ; Inflammation/metabolism ; Neanderthals/genetics ; Peptidyl-Dipeptidase A/genetics ; Peptidyl-Dipeptidase A/metabolism ; Polymorphism, Genetic ; Risk Factors ; Severity of Illness Index
Chemical Substances	HLA Antigens ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2021-05-08
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22095000
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Article ; Online: TIP60 Complex Inhibits Hepatitis B Virus Transcription.

Nishitsuji, Hironori / Ujino, Saneyuki / Harada, Keisuke / Shimotohno, Kunitada

Journal of virology

2018 Volume 92, Issue 6

Abstract: Hepatitis B virus (HBV) is a global major health problem, with over one million deaths annually caused by chronic liver damage. Understanding host factors that modulate HBV replication may aid the development of anti-HBV therapies. Our recent genome-wide ...

Abstract	Hepatitis B virus (HBV) is a global major health problem, with over one million deaths annually caused by chronic liver damage. Understanding host factors that modulate HBV replication may aid the development of anti-HBV therapies. Our recent genome-wide small interfering RNA screen using recombinant HBV demonstrated that TIP60 inhibited HBV infection. Here, we show that TIP60 complex contributes to anti-HBV defense. The TIP60 complex bound to the HBV promoter and suppressed HBV transcription driven by the precore/core promoter. The silencing of EP400, TRRAP, BAF53a, RUVBL1, and RUVBL2, which form the TIP60 complex, also resulted in increased HBV transcription. These results contribute to our enhanced understanding of the molecular mechanism of HBV transcription associated with the chromatin structure of HBV covalently closed circular DNA (cccDNA). Exploiting these intrinsic cellular defenses might help develop new anti-HBV agents.
MeSH term(s)	Acetylation ; Chromatin/genetics ; Chromatin/metabolism ; Chromatin/pathology ; Chromatin/virology ; Hep G2 Cells ; Hepatitis B/genetics ; Hepatitis B/metabolism ; Hepatitis B/pathology ; Hepatitis B virus/physiology ; Histones/genetics ; Histones/metabolism ; Humans ; Lysine Acetyltransferase 5/genetics ; Lysine Acetyltransferase 5/metabolism ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription, Genetic ; Virus Replication/physiology
Chemical Substances	BRD4 protein, human ; Chromatin ; Histones ; Multiprotein Complexes ; Nuclear Proteins ; Transcription Factors ; KAT5 protein, human (EC 2.3.1.48) ; Lysine Acetyltransferase 5 (EC 2.3.1.48)
Language	English
Publishing date	2018-02-26
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.01788-17
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Zs.A 609: Show issues

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Article ; Online: Pegylated interferon therapy-related microRNA-6126 downregulates sodium taurocholate cotransporting polypeptide expression in hepatocytes.

Fujita, Koji / Nishitsuji, Hironori / Iwama, Hisakazu / Tadokoro, Tomoko / Morishita, Asahiro / Mimura, Shima / Ono, Masafumi / Himoto, Takashi / Shimotohno, Kunitada / Masaki, Tsutomu

Gene

2022 Volume 853, Page(s) 147068

Abstract: Hepatitis B virus (HBV) infection is one of the most serious global health problems. Our previous data using an in vitro assay revealed that miR-6126 suppressed the extracellular HBs antigen level, suggesting that miR-6126 had potential to suppress viral ...

Abstract	Hepatitis B virus (HBV) infection is one of the most serious global health problems. Our previous data using an in vitro assay revealed that miR-6126 suppressed the extracellular HBs antigen level, suggesting that miR-6126 had potential to suppress viral activity of HBV. In the current study, we aimed to clarify whether miR-6126 downregulated the expression level of sodium taurocholate cotransporting polypeptide (NTCP), a host cell receptor required for HBV entry. In brief, HepG2-NTCP cells were utilized to evaluate the expression level of NTCP and the PreS1 attachment to NTCP after transfection with miR-6126. The protein expression level of NTCP was evaluated using Western blot analysis and immunostaining. In addition to HepG2-NTCP cells, PXB cells were also utilized to validate inhibitory effect of miR-6126 on PreS1 attachment. The HBs antigen level in the culture supernatant was measured to evaluate reduction of HBV entry into hepatocytes. The stability of NTCP mRNA was evaluated to ascertain the cause of the downregulation of NTCP mRNA. The expression profile of messenger RNAs was evaluated using next-generation sequencing to search for direct targets of miR-6126. Consequently, transfection of miR-6126 decreased the NTCP expression level in HepG2-NTCP cells. Attachment of the PreS1 probe on the cell surface decreased in HepG2-NTCP cells and PXB cells, primary human hepatocytes. HBs antigen level in the culture supernatant also declined in PXB cells. Stability of NTCP mRNA was reduced by miR-6126 transfection in HepG2 cells. In conclusion, miR-6126 downregulated the expression of NTCP mRNA, which contributed to the inhibition of HBV entry into hepatocytes exerted by miR-6126.
Language	English
Publishing date	2022-11-24
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	391792-7
ISSN	1879-0038 ; 0378-1119
ISSN (online)	1879-0038
ISSN	0378-1119
DOI	10.1016/j.gene.2022.147068
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