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Article ; Online: The PACS-2 protein and trafficking motifs in CCHFV Gn and Gc cytoplasmic tails govern CCHFV assembly.

Gautam, Anupriya / Lalande, Alexandre / Ritter, Maureen / Freitas, Natalia / Lerolle, Solène / Canus, Lola / Amirache, Fouzia / Lotteau, Vincent / Legros, Vincent / Cosset, François-Loïc / Mathieu, Cyrille / Boson, Bertrand

Emerging microbes & infections

2024 , Page(s) 2348508

Abstract: ... ...

Abstract	Abstract
Language	English
Publishing date	2024-04-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	2681359-2
ISSN	2222-1751 ; 2222-1751
ISSN (online)	2222-1751
ISSN	2222-1751
DOI	10.1080/22221751.2024.2348508
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Nup98 Is Subverted from Annulate Lamellae by Hepatitis C Virus Core Protein to Foster Viral Assembly.

Boson, Bertrand / Mialon, Chloé / Schichl, Konstanze / Denolly, Solène / Cosset, François-Loïc

mBio

2022 Volume 13, Issue 2, Page(s) e0292321

Abstract: Nup98, an essential component of the nuclear pore that also participates in annulate lamella pore structures localized in the cytosol, is involved in hepatitis C virus (HCV) assembly. Here, we combined confocal microscopy and biochemical assays to study ... ...

Abstract	Nup98, an essential component of the nuclear pore that also participates in annulate lamella pore structures localized in the cytosol, is involved in hepatitis C virus (HCV) assembly. Here, we combined confocal microscopy and biochemical assays to study the interplay between Nup98, core (i.e., the HCV capsid protein), and viral genomes. Our results show that in HCV-infected cells, core protein is necessary and sufficient to induce relocalization of Nup98 from annulate lamellae to lipid droplet-apposed areas in which core/NS5A and HCV genomic RNA [(+)RNA] are clustered to promote viral assembly. Furthermore, we found that Nup98 interacts with HCV RNA and that upon Nup98 downregulation, the viral (+)RNA genome was specifically excluded from areas that contain active translating ribosomes and the core and NS5A proteins. Altogether, these results indicate that Nup98 is recruited by HCV core from annulate lamellae to viral assembly sites to locally increase the concentration of (+)RNA genome, which may favor its encapsidation into nascent virions.
MeSH term(s)	Hepacivirus/genetics ; Hepatitis C ; Humans ; Nuclear Pore Complex Proteins/genetics ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Viral Core Proteins/genetics ; Viral Core Proteins/metabolism ; Virus Assembly/physiology
Chemical Substances	Nuclear Pore Complex Proteins ; Nup98 protein, human ; RNA, Viral ; Viral Core Proteins
Language	English
Publishing date	2022-03-08
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.02923-21
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Article ; Online: Low-density hepatitis C virus infectious particles are protected from oxidation by secreted cellular proteins.

Granier, Christelle / Toesca, Johan / Mialon, Chloé / Ritter, Maureen / Freitas, Natalia / Boson, Bertrand / Pécheur, Eve-Isabelle / Cosset, François-Loïc / Denolly, Solène

mBio

2023 Volume 14, Issue 5, Page(s) e0154923

Abstract: Importance: Assessments of viral stability on surfaces or in body fluids under different environmental conditions and/or temperatures are often performed, as they are key to understanding the routes and parameters of viral transmission and to providing ... ...

Abstract	Importance: Assessments of viral stability on surfaces or in body fluids under different environmental conditions and/or temperatures are often performed, as they are key to understanding the routes and parameters of viral transmission and to providing clues on the epidemiology of infections. However, for most viruses, the mechanisms of inactivation vs stability of viral particles remain poorly defined. Although they are structurally diverse, with different compositions, sizes, and shapes, enveloped viruses are generally less stable than non-enveloped viruses, pointing out the role of envelopes themselves in virus lability. In this report, we investigated the properties of hepatitis C virus (HCV) particles with regards to their stability. We found that, compared to alternative enveloped viruses such as Dengue virus (DENV), severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), hepatitis delta virus (HDV), and Crimean-Congo hemorrhagic fever virus (CCHFV) that infect the liver, HCV particles are intrinsically labile. We determined the mechanisms that drastically alter their specific infectivity through oxidation of their lipids, and we highlighted that they are protected from lipid oxidation by secreted cellular proteins, which can protect their membrane fusion capacity and overall infectivity.
MeSH term(s)	Humans ; Hepacivirus ; Hemorrhagic Fever Virus, Crimean-Congo/physiology ; Hepatitis C/metabolism
Language	English
Publishing date	2023-09-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.01549-23
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Article ; Online: Overview of HCV Life Cycle with a Special Focus on Current and Possible Future Antiviral Targets.

Alazard-Dany, Nathalie / Denolly, Solène / Boson, Bertrand / Cosset, François-Loïc

Viruses

2019 Volume 11, Issue 1

Abstract: Hepatitis C infection is the leading cause of liver diseases worldwide and a major health concern that affects an estimated 3% of the global population. Novel therapies available since 2014 and 2017 are very efficient and the WHO considers HCV ... ...

Abstract	Hepatitis C infection is the leading cause of liver diseases worldwide and a major health concern that affects an estimated 3% of the global population. Novel therapies available since 2014 and 2017 are very efficient and the WHO considers HCV eradication possible by the year 2030. These treatments are based on the so-called direct acting antivirals (DAAs) that have been developed through research efforts by academia and industry since the 1990s. After a brief overview of the HCV life cycle, we describe here the functions of the different targets of current DAAs, the mode of action of these DAAs and potential future inhibitors.
MeSH term(s)	Antiviral Agents/pharmacology ; Hepacivirus/drug effects ; Hepacivirus/physiology ; Hepatitis C/drug therapy ; Humans ; Molecular Targeted Therapy ; Protease Inhibitors/pharmacology
Chemical Substances	Antiviral Agents ; Protease Inhibitors
Language	English
Publishing date	2019-01-06
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v11010030
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Article ; Online: HCV Interplay with Lipoproteins: Inside or Outside the Cells?

Cosset, François-Loïc / Mialon, Chloé / Boson, Bertrand / Granier, Christelle / Denolly, Solène

Viruses

2020 Volume 12, Issue 4

Abstract: Hepatitis C virus (HCV) infection is a major public health issue leading to chronic liver diseases. HCV particles are unique owing to their particular lipid composition, namely the incorporation of neutral lipids and apolipoproteins. The mechanism of ... ...

Abstract	Hepatitis C virus (HCV) infection is a major public health issue leading to chronic liver diseases. HCV particles are unique owing to their particular lipid composition, namely the incorporation of neutral lipids and apolipoproteins. The mechanism of association between HCV virion components and these lipoproteins factors remains poorly understood as well as its impact in subsequent steps of the viral life cycle, such as entry into cells. It was proposed that the lipoprotein biogenesis pathway is involved in HCV morphogenesis; yet, recent evidence indicated that HCV particles can mature and evolve biochemically in the extracellular medium after egress. In addition, several viral, cellular and blood components have been shown to influence and regulate this specific association. Finally, this specific structure and composition of HCV particles was found to influence entry into cells as well as their stability and sensitivity to neutralizing antibodies. Due to its specific particle composition, studying the association of HCV particles with lipoproteins remains an important goal towards the rational design of a protective vaccine.
MeSH term(s)	Animals ; Endoplasmic Reticulum/metabolism ; Hepacivirus/physiology ; Hepatitis C/immunology ; Hepatitis C/metabolism ; Hepatitis C/virology ; Host-Pathogen Interactions ; Humans ; Lipid Metabolism ; Lipoproteins/biosynthesis ; Lipoproteins/metabolism ; Protein Transport ; Signal Transduction ; Virion ; Virus Assembly ; Virus Internalization
Chemical Substances	Lipoproteins
Language	English
Publishing date	2020-04-12
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v12040434
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Article ; Online: Hepatitis C virus core protein uses triacylglycerols to fold onto the endoplasmic reticulum membrane.

Ajjaji, Dalila / Ben M'barek, Kalthoum / Boson, Bertrand / Omrane, Mohyeddine / Gassama-Diagne, Ama / Blaud, Magali / Penin, François / Diaz, Elise / Ducos, Bertrand / Cosset, François-Loïc / Thiam, Abdou Rachid

Traffic (Copenhagen, Denmark)

2021 Volume 23, Issue 1, Page(s) 63–80

Abstract: Lipid droplets (LDs) are involved in viral infections, but exactly how remains unclear. Here, we study the hepatitis C virus (HCV) whose core capsid protein binds to LDs but is also involved in the assembly of virions at the endoplasmic reticulum (ER) ... ...

Abstract	Lipid droplets (LDs) are involved in viral infections, but exactly how remains unclear. Here, we study the hepatitis C virus (HCV) whose core capsid protein binds to LDs but is also involved in the assembly of virions at the endoplasmic reticulum (ER) bilayer. We found that the amphipathic helix-containing domain of core, D2, senses triglycerides (TGs) rather than LDs per se. In the absence of LDs, D2 can bind to the ER membrane but only if TG molecules are present in the bilayer. Accordingly, the pharmacological inhibition of the diacylglycerol O-acyltransferase enzymes, mediating TG synthesis in the ER, inhibits D2 association with the bilayer. We found that TG molecules enable D2 to fold into alpha helices. Sequence analysis reveals that D2 resembles the apoE lipid-binding region. Our data support that TG in LDs promotes the folding of core, which subsequently relocalizes to contiguous ER regions. During this motion, core may carry TG molecules to these regions where HCV lipoviroparticles likely assemble. Consistent with this model, the inhibition of Arf1/COPI, which decreases LD surface accessibility to proteins and ER-LD material exchange, severely impedes the assembly of virions. Altogether, our data uncover a critical function of TG in the folding of core and HCV replication and reveals, more broadly, how TG accumulation in the ER may provoke the binding of soluble amphipathic helix-containing proteins to the ER bilayer.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Hepacivirus/physiology ; Hepatitis C/metabolism ; Humans ; Lipid Droplets/metabolism ; Triglycerides/metabolism ; Viral Core Proteins/metabolism
Chemical Substances	Triglycerides ; Viral Core Proteins
Language	English
Publishing date	2021-11-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12825
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Article: HCV Interplay with Lipoproteins: Inside or Outside the Cells?

Cosset, François-Loïc / Mialon, Chloé / Boson, Bertrand / Granier, Christelle / Denolly, Solène

Viruses. 2020 Apr. 12, v. 12, no. 4

2020

Abstract	Hepatitis C virus (HCV) infection is a major public health issue leading to chronic liver diseases. HCV particles are unique owing to their particular lipid composition, namely the incorporation of neutral lipids and apolipoproteins. The mechanism of association between HCV virion components and these lipoproteins factors remains poorly understood as well as its impact in subsequent steps of the viral life cycle, such as entry into cells. It was proposed that the lipoprotein biogenesis pathway is involved in HCV morphogenesis; yet, recent evidence indicated that HCV particles can mature and evolve biochemically in the extracellular medium after egress. In addition, several viral, cellular and blood components have been shown to influence and regulate this specific association. Finally, this specific structure and composition of HCV particles was found to influence entry into cells as well as their stability and sensitivity to neutralizing antibodies. Due to its specific particle composition, studying the association of HCV particles with lipoproteins remains an important goal towards the rational design of a protective vaccine.
Keywords	Hepatitis C virus ; apolipoproteins ; biogenesis ; blood ; lipid composition ; liver diseases ; morphogenesis ; neutralizing antibodies ; public health ; triacylglycerols ; vaccines ; virion
Language	English
Dates of publication	2020-0412
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v12040434
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: The SARS-CoV-2 envelope and membrane proteins modulate maturation and retention of the spike protein, allowing assembly of virus-like particles.

Boson, Bertrand / Legros, Vincent / Zhou, Bingjie / Siret, Eglantine / Mathieu, Cyrille / Cosset, François-Loïc / Lavillette, Dimitri / Denolly, Solène

The Journal of biological chemistry

2020 Volume 296, Page(s) 100111

Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a β-coronavirus, is the causative agent of the COVID-19 pandemic. Like for other coronaviruses, its particles are composed of four structural proteins: spike (S), envelope (E), membrane (M) ...

Abstract	The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a β-coronavirus, is the causative agent of the COVID-19 pandemic. Like for other coronaviruses, its particles are composed of four structural proteins: spike (S), envelope (E), membrane (M), and nucleoprotein (N) proteins. The involvement of each of these proteins and their interactions are critical for assembly and production of β-coronavirus particles. Here, we sought to characterize the interplay of SARS-CoV-2 structural proteins during the viral assembly process. By combining biochemical and imaging assays in infected versus transfected cells, we show that E and M regulate intracellular trafficking of S as well as its intracellular processing. Indeed, the imaging data reveal that S is relocalized at endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC) or Golgi compartments upon coexpression of E or M, as observed in SARS-CoV-2-infected cells, which prevents syncytia formation. We show that a C-terminal retrieval motif in the cytoplasmic tail of S is required for its M-mediated retention in the ERGIC, whereas E induces S retention by modulating the cell secretory pathway. We also highlight that E and M induce a specific maturation of N-glycosylation of S, independently of the regulation of its localization, with a profile that is observed both in infected cells and in purified viral particles. Finally, we show that E, M, and N are required for optimal production of virus-like-particles. Altogether, these results highlight how E and M proteins may influence the properties of S proteins and promote the assembly of SARS-CoV-2 viral particles.
MeSH term(s)	Animals ; Biomimetic Materials/chemistry ; Biomimetic Materials/metabolism ; Cell Line, Tumor ; Chlorocebus aethiops ; Coronavirus Envelope Proteins/genetics ; Coronavirus Envelope Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; Endoplasmic Reticulum/virology ; Gene Expression ; Golgi Apparatus/metabolism ; Golgi Apparatus/ultrastructure ; Golgi Apparatus/virology ; HEK293 Cells ; Hepatocytes/metabolism ; Hepatocytes/ultrastructure ; Hepatocytes/virology ; Host-Pathogen Interactions/genetics ; Humans ; Nucleocapsid Proteins/genetics ; Nucleocapsid Proteins/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; SARS-CoV-2/genetics ; SARS-CoV-2/growth & development ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Vero Cells ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/metabolism ; Virion/genetics ; Virion/growth & development ; Virion/metabolism ; Virus Assembly/physiology ; Virus Internalization ; Virus Release/physiology
Chemical Substances	Coronavirus Envelope Proteins ; Nucleocapsid Proteins ; Recombinant Proteins ; Spike Glycoprotein, Coronavirus ; Viral Matrix Proteins ; envelope protein, SARS-CoV-2 ; membrane protein, SARS-CoV-2 ; spike protein, SARS-CoV-2
Language	English
Publishing date	2020-12-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.016175
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Article ; Online: Detection of SARS-CoV-2 in two cats during the second wave of the COVID-19 pandemic in France.

Fritz, Matthieu / Nesi, Nicolas / Denolly, Solène / Boson, Bertrand / Legros, Vincent / Rosolen, Serge G / Briend-Marchal, Alexandra / Ar Gouilh, Meriadeg / Leroy, Eric M

Veterinary medicine and science

2021 Volume 8, Issue 1, Page(s) 14–20

Abstract: Although there are several reports in the literature of SARS-CoV-2 infection in cats, few SARS-CoV-2 sequences from infected cats have been published. In this study, SARS-CoV-2 infection was evaluated in two cats by clinical observation, molecular ... ...

Abstract	Although there are several reports in the literature of SARS-CoV-2 infection in cats, few SARS-CoV-2 sequences from infected cats have been published. In this study, SARS-CoV-2 infection was evaluated in two cats by clinical observation, molecular biology (qPCR and NGS), and serology (microsphere immunoassay and seroneutralization). Following the observation of symptomatic SARS-CoV-2 infection in two cats, infection status was confirmed by RT-qPCR and, in one cat, serological analysis for antibodies against N-protein and S-protein, as well as neutralizing antibodies. Comparative analysis of five SARS-CoV-2 sequence fragments obtained from one of the cats showed that this infection was not with one of the three recently emerged variants of SARS-CoV-2. This study provides additional information on the clinical, molecular, and serological aspects of SARS-CoV-2 infection in cats.
MeSH term(s)	Animals ; COVID-19/veterinary ; Cat Diseases/epidemiology ; Cats ; France/epidemiology ; Pandemics ; SARS-CoV-2
Language	English
Publishing date	2021-10-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2819409-3
ISSN	2053-1095 ; 2053-1095
ISSN (online)	2053-1095
ISSN	2053-1095
DOI	10.1002/vms3.638
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Article ; Online: Detection of SARS‐CoV‐2 in two cats during the second wave of the COVID‐19 pandemic in France

Matthieu Fritz / Nicolas Nesi / Solène Denolly / Bertrand Boson / Vincent Legros / Serge G. Rosolen / Alexandra Briend‐Marchal / Meriadeg Ar Gouilh / Eric M. Leroy

Veterinary Medicine and Science, Vol 8, Iss 1, Pp 14-

2022 Volume 20

Abstract: Abstract Although there are several reports in the literature of SARS‐CoV‐2 infection in cats, few SARS‐CoV‐2 sequences from infected cats have been published. In this study, SARS‐CoV‐2 infection was evaluated in two cats by clinical observation, ... ...

Abstract	Abstract Although there are several reports in the literature of SARS‐CoV‐2 infection in cats, few SARS‐CoV‐2 sequences from infected cats have been published. In this study, SARS‐CoV‐2 infection was evaluated in two cats by clinical observation, molecular biology (qPCR and NGS), and serology (microsphere immunoassay and seroneutralization). Following the observation of symptomatic SARS‐CoV‐2 infection in two cats, infection status was confirmed by RT‐qPCR and, in one cat, serological analysis for antibodies against N‐protein and S‐protein, as well as neutralizing antibodies. Comparative analysis of five SARS‐CoV‐2 sequence fragments obtained from one of the cats showed that this infection was not with one of the three recently emerged variants of SARS‐CoV‐2. This study provides additional information on the clinical, molecular, and serological aspects of SARS‐CoV‐2 infection in cats.
Keywords	cats ; mild‐respiratory clinical signs ; NGS ; One Health ; SARS‐CoV‐2 ; serology ; Veterinary medicine ; SF600-1100
Language	English
Publishing date	2022-01-01T00:00:00Z
Publisher	Wiley
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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