LIVIVO - Search results -

Search results

Result 1 - 10 of total 38

Search options

Article ; Online: La mitophagie : une stratégie du virus d’Epstein-Barr pour échapper à l’immunité innée.

Glon, Damien / Lussignol, Marion / Esclatine, Audrey

2020 Volume 36, Issue 11, Page(s) 990–993

Title translation	Mitophagy: a strategy of the Epstein-Barr virus to evade innate immunity.
MeSH term(s)	Animals ; Epstein-Barr Virus Infections/immunology ; Epstein-Barr Virus Infections/pathology ; Herpesvirus 4, Human/immunology ; Humans ; Immune Evasion/physiology ; Immunity, Innate/physiology ; Mitophagy/physiology
Language	French
Publishing date	2020-11-05
Publishing country	France
Document type	News
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2020185
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 2872: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Commercially Available Eye Drops Containing Trehalose Protect Against Dry Conditions via Autophagy Induction.

Hernandez, Eva / Taisne, Clémence / Lussignol, Marion / Esclatine, Audrey / Labetoulle, Marc

Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics

2021 Volume 37, Issue 7, Page(s) 386–393

Abstract: Purpose: ...

Abstract	Purpose:
MeSH term(s)	Autophagy/drug effects ; Dry Eye Syndromes/drug therapy ; Dry Eye Syndromes/pathology ; HeLa Cells ; Humans ; Lubricant Eye Drops/pharmacology ; Trehalose/pharmacology ; Tumor Cells, Cultured
Chemical Substances	Lubricant Eye Drops ; Trehalose (B8WCK70T7I)
Language	English
Publishing date	2021-07-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	1237021-6
ISSN	1557-7732 ; 1080-7683
ISSN (online)	1557-7732
ISSN	1080-7683
DOI	10.1089/jop.2020.0119
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2099: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Herpesvirus and Autophagy: "All Right, Everybody Be Cool, This Is a Robbery!"

Lussignol, Marion / Esclatine, Audrey

Viruses

2017 Volume 9, Issue 12

Abstract: Autophagy is an essential vacuolar process of the cell, leading to lysosomal degradation and recycling of proteins and organelles, which is extremely important in maintaining homeostasis. Multiple roles have been now associated with autophagy, in ... ...

Abstract	Autophagy is an essential vacuolar process of the cell, leading to lysosomal degradation and recycling of proteins and organelles, which is extremely important in maintaining homeostasis. Multiple roles have been now associated with autophagy, in particular a pro-survival role in nutrient starvation or in stressful environments, a role in life span extension, in development, or in innate and adaptive immunity. This cellular process can also take over microorganisms or viral proteins inside autophagosomes and degrade them directly in autolysosomes and is then called xenophagy and virophagy, respectively. Several Herpesviruses have developed strategies to escape this degradation, by expression of specific anti-autophagic proteins. However, we are increasingly discovering that Herpesviruses hijack autophagy, rather than just fight it. This beneficial effect is obvious since inhibition of autophagy will lead to decreased viral titers for human cytomegalovirus (HCMV), Epstein-Barr virus (EBV) or Varicella-Zoster virus (VZV), for example. Conversely, autophagy stimulation will improve viral multiplication. The autophagic machinery can be used in whole or in part, and can optimize viral propagation or persistence. Some viruses block maturation of autophagosomes to avoid the degradation step, then autophagosomal membranes are used to contribute to the envelopment and/or the egress of viral particles. On the other hand, VZV stimulates the whole process of autophagy to subvert it in order to use vesicles containing ATG (autophagy-related) proteins and resembling amphisomes for their transport in the cytoplasm. During latency, autophagy can also be activated by latent proteins encoded by different oncogenic Herpesviruses to promote cell survival and achieve long term viral persistence in vivo. Finally, reactivation of gammaherpesvirus Murid Herpesvirus 68 (MHV68) in mice appears to be positively modulated by autophagy, in order to control the level of inflammation. Therefore, Herpesviruses appear to behave more like thieves than fugitives.
MeSH term(s)	Animals ; Autophagy ; Herpesviridae/physiology ; Host-Pathogen Interactions ; Humans ; Virus Latency ; Virus Release ; Virus Replication
Language	English
Publishing date	2017--04
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/v9120372
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Autophagic Degradation Is Involved in Cell Protection against Ricin Toxin.

Wu, Yu / Taisne, Clémence / Mahtal, Nassim / Forrester, Alison / Lussignol, Marion / Cintrat, Jean-Christophe / Esclatine, Audrey / Gillet, Daniel / Barbier, Julien

Toxins

2023 Volume 15, Issue 5

Abstract: Autophagy is a complex and highly regulated degradative process, which acts as a survival pathway in response to cellular stress, starvation and pathogen infection. Ricin toxin is a plant toxin produced by the castor bean and classified as a category B ... ...

Abstract	Autophagy is a complex and highly regulated degradative process, which acts as a survival pathway in response to cellular stress, starvation and pathogen infection. Ricin toxin is a plant toxin produced by the castor bean and classified as a category B biothreat agent. Ricin toxin inhibits cellular protein synthesis by catalytically inactivating ribosomes, leading to cell death. Currently, there is no licensed treatment for patients exposed to ricin. Ricin-induced apoptosis has been extensively studied; however, whether its intoxication via protein synthesis inhibition affects autophagy is not yet resolved. In this work, we demonstrated that ricin intoxication is accompanied by its own autophagic degradation in mammalian cells. Autophagy deficiency, by knocking down ATG5, attenuates ricin degradation, thus aggravating ricin-induced cytotoxicity. Additionally, the autophagy inducer SMER28 (Small Molecule Enhancer 28) partially protects cells against ricin cytotoxicity, an effect not observed in autophagy-deficient cells. These results demonstrate that autophagic degradation acts as a survival response of cells against ricin intoxication. This suggests that stimulation of autophagic degradation may be a strategy to counteract ricin intoxication.
MeSH term(s)	Animals ; Humans ; Ricin/toxicity ; Ricin/metabolism ; Cytoprotection ; Proteins ; Apoptosis ; Autophagy ; Mammals/metabolism
Chemical Substances	Ricin (9009-86-3) ; Proteins
Language	English
Publishing date	2023-04-23
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2518395-3
ISSN	2072-6651 ; 2072-6651
ISSN (online)	2072-6651
ISSN	2072-6651
DOI	10.3390/toxins15050304
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Human cytomegalovirus hijacks the autophagic machinery and LC3 homologs in order to optimize cytoplasmic envelopment of mature infectious particles.

Taisne, Clémence / Lussignol, Marion / Hernandez, Eva / Moris, Arnaud / Mouna, Lina / Esclatine, Audrey

Scientific reports

2019 Volume 9, Issue 1, Page(s) 4560

Abstract: During its life cycle, Human cytomegalovirus (HCMV) tightly modulates autophagy, a vesicular pathway allowing degradation and recycling of cellular components. To study the interplay between autophagy and the viral life cycle, we established various ... ...

Abstract	During its life cycle, Human cytomegalovirus (HCMV) tightly modulates autophagy, a vesicular pathway allowing degradation and recycling of cellular components. To study the interplay between autophagy and the viral life cycle, we established various autophagy-deficient human fibroblastic cell lines. By knocking down the expression or activity of five autophagy-related proteins, we confirmed the proviral function that the autophagic machinery exerts on HCMV production. Using 3D reconstruction from confocal microscopy and electron microscopy, we demonstrated that lipidated LC3-positive vesicles accumulated at the viral assembly compartment (vAC). The vAC is a juxtanuclear ring-shaped structure containing several organelles and membranes, where assembly and final envelopment of HCMV particles occur. Two LC3 homologs, GABARAPL1 and GATE16, also accumulated during HCMV infection and were associated with the vAC, in proximity with fragmented Golgi stacks. Additionally, we observed the formation of a pre-assembly compartment (PrAC) in infected cells, which consists of a juxtanuclear structure containing both fragmented Golgi and LC3-positive vesicles. Finally, we showed that highly purified extracellular viral particles were associated with various autophagy proteins. Our results thus suggest that autophagy machinery participates to the final cytoplasmic envelopment of HCMV viral particles into the vAC and that autophagy-related proteins can be spotted in the virions.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Autophagy ; Autophagy-Related Protein 8 Family/genetics ; Autophagy-Related Protein 8 Family/metabolism ; Cells, Cultured ; Cytomegalovirus/pathogenicity ; Cytomegalovirus Infections/genetics ; Cytomegalovirus Infections/metabolism ; Cytomegalovirus Infections/virology ; Cytosol/virology ; Endosomes/virology ; Fibroblasts/virology ; Humans ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Virion ; Virus Assembly ; Virus Replication
Chemical Substances	Adaptor Proteins, Signal Transducing ; Autophagy-Related Protein 8 Family ; GABARAPL1 protein, human ; GABARAPL2 protein, human ; Microtubule-Associated Proteins
Language	English
Publishing date	2019-03-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-41029-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy.

Beilstein, Frauke / Cohen, Gary H / Eisenberg, Roselyn J / Nicolas, Valérie / Esclatine, Audrey / Pasdeloup, David

PLoS pathogens

2019 Volume 15, Issue 12, Page(s) e1008209

Abstract: The processes of cell attachment and membrane fusion of Herpes Simplex Virus 1 involve many different envelope glycoproteins. Viral proteins gC and gD bind to cellular receptors. Upon binding, gD activates the gH/gL complex which in turn activates gB to ... ...

Abstract	The processes of cell attachment and membrane fusion of Herpes Simplex Virus 1 involve many different envelope glycoproteins. Viral proteins gC and gD bind to cellular receptors. Upon binding, gD activates the gH/gL complex which in turn activates gB to trigger membrane fusion. Thus, these proteins must be located at the point of contact between cellular and viral envelopes to interact and allow fusion. Using super-resolution microscopy, we show that gB, gH/gL and most of gC are distributed evenly round purified virions. In contrast, gD localizes essentially as clusters which are distinct from gB and gH/gL. Upon cell binding, we observe that all glycoproteins, including gD, have a similar ring-like pattern, but the diameter of these rings was significantly smaller than those observed on cell-free viruses. We also observe that contrary to cell-free particles, gD mostly colocalizes with other glycoproteins on cell-bound particles. The differing patterns of localization of gD between cell-free and cell-bound viruses indicates that gD can be reorganized on the viral envelope following either a possible maturation of the viral particle or its adsorption to the cell. This redistribution of glycoproteins upon cell attachment could contribute to initiate the cascade of activations leading to membrane fusion.
MeSH term(s)	Cell Line ; Glycoproteins/metabolism ; Glycoproteins/ultrastructure ; Herpesvirus 1, Human/metabolism ; Herpesvirus 1, Human/ultrastructure ; Humans ; Microscopy/methods ; Viral Envelope Proteins/metabolism ; Viral Envelope Proteins/ultrastructure ; Virion/metabolism ; Virion/ultrastructure ; Virus Attachment ; Virus Internalization
Chemical Substances	Glycoproteins ; Viral Envelope Proteins
Language	English
Publishing date	2019-12-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1008209
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Membrane protective role of autophagic machinery during infection of epithelial cells by

Lapaquette, Pierre / Ducreux, Amandine / Basmaciyan, Louise / Paradis, Tracy / Bon, Fabienne / Bataille, Amandine / Winckler, Pascale / Hube, Bernhard / d'Enfert, Christophe / Esclatine, Audrey / Dubus, Elisabeth / Bringer, Marie-Agnès / Morel, Etienne / Dalle, Frédéric

Gut microbes

2022 Volume 14, Issue 1, Page(s) 2004798

Abstract: ... Candida ... ...

Abstract	Candida albicans
MeSH term(s)	Autophagy ; Autophagy-Related Protein 5/genetics ; Autophagy-Related Protein 5/metabolism ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Candida albicans/genetics ; Candida albicans/physiology ; Candidiasis/genetics ; Candidiasis/metabolism ; Candidiasis/microbiology ; Candidiasis/physiopathology ; Cell Membrane/microbiology ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Epithelial Cells/microbiology ; Gastrointestinal Microbiome ; Host-Pathogen Interactions ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Phosphate-Binding Proteins/genetics ; Phosphate-Binding Proteins/metabolism
Chemical Substances	ATG16L1 protein, human ; Autophagy-Related Protein 5 ; Autophagy-Related Proteins ; Membrane Proteins ; Phosphate-Binding Proteins ; WIPI2 protein, human
Language	English
Publishing date	2022-01-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1949-0984
ISSN (online)	1949-0984
DOI	10.1080/19490976.2021.2004798
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Essential role of hyperacetylated microtubules in innate immunity escape orchestrated by the EBV-encoded BHRF1 protein.

Glon, Damien / Vilmen, Géraldine / Perdiz, Daniel / Hernandez, Eva / Beauclair, Guillaume / Quignon, Frédérique / Berlioz-Torrent, Clarisse / Maréchal, Vincent / Poüs, Christian / Lussignol, Marion / Esclatine, Audrey

PLoS pathogens

2022 Volume 18, Issue 3, Page(s) e1010371

Abstract: Innate immunity constitutes the first line of defense against viruses, in which mitochondria play an important role in the induction of the interferon (IFN) response. BHRF1, a multifunctional viral protein expressed during Epstein-Barr virus reactivation, ...

Abstract	Innate immunity constitutes the first line of defense against viruses, in which mitochondria play an important role in the induction of the interferon (IFN) response. BHRF1, a multifunctional viral protein expressed during Epstein-Barr virus reactivation, modulates mitochondrial dynamics and disrupts the IFN signaling pathway. Mitochondria are mobile organelles that move through the cytoplasm thanks to the cytoskeleton and in particular the microtubule (MT) network. MTs undergo various post-translational modifications, among them tubulin acetylation. In this study, we demonstrated that BHRF1 induces MT hyperacetylation to escape innate immunity. Indeed, the expression of BHRF1 induces the clustering of shortened mitochondria next to the nucleus. This "mito-aggresome" is organized around the centrosome and its formation is MT-dependent. We also observed that the α-tubulin acetyltransferase ATAT1 interacts with BHRF1. Using ATAT1 knockdown or a non-acetylatable α-tubulin mutant, we demonstrated that this hyperacetylation is necessary for the mito-aggresome formation. Similar results were observed during EBV reactivation. We investigated the mechanism leading to the clustering of mitochondria, and we identified dyneins as motors that are required for mitochondrial clustering. Finally, we demonstrated that BHRF1 needs MT hyperacetylation to block the induction of the IFN response. Moreover, the loss of MT hyperacetylation blocks the localization of autophagosomes close to the mito-aggresome, impeding BHRF1 to initiate mitophagy, which is essential to inhibiting the signaling pathway. Therefore, our results reveal the role of the MT network, and its acetylation level, in the induction of a pro-viral mitophagy.
MeSH term(s)	Epstein-Barr Virus Infections/immunology ; Herpesvirus 4, Human/physiology ; Humans ; Immunity, Innate ; Microtubules/metabolism ; Mitophagy ; Tubulin/metabolism ; Viral Proteins/metabolism
Chemical Substances	BHRF1 protein, Human herpesvirus 4 ; Tubulin ; Viral Proteins
Language	English
Publishing date	2022-03-11
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010371
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Autophagy Receptors in the presentation of Viral antigens by MHC-II molecules

Pereira, Mathias / Richetta, Clémence / Ghosh, Michael / Rosoy, Elina / Bertrand, Lisa / Ramirez, Cecilia / Jeger-Madiot, Raphael / Faure, Mathias / Esclatine, Audrey / Stevanovic, Stefan / Graff-Dubois, Stéphanie / Manoury, Bénédicte / Moris, Arnaud

Molecular immunology. 2022 Oct., v. 150

2022

Abstract: CD4+ T lymphocytes play a major role in the establishment and maintenance of antiviral immunity. CD4+ T cells are activated by antigenic peptides, derived from pathogens, presented by MHC-II molecules. It is still widely assumed that CD4+ T cells ... ...

Abstract	CD4+ T lymphocytes play a major role in the establishment and maintenance of antiviral immunity. CD4+ T cells are activated by antigenic peptides, derived from pathogens, presented by MHC-II molecules. It is still widely assumed that CD4+ T cells recognize epitopes derived solely from exogenous viral particles or proteins. However, alternative sources of MHC-II-restricted antigens have been described. We showed that HIV-infected dendritic cells present MHC-II–restricted epitopes derived from newly synthesized proteins to HIV-specific CD4+ T cells. In fact, we confirmed that multiple cellular degradation pathways lead to endogenous presentation of MHC-II-restricted viral antigens, the generation of some viral epitopes being dependent and/or -independent on macroautophagy (herein referred as autophagy). We are charactering further these MHC-II-restricted endogenous presentation pathways. In particular, using RNA silencing, we asked whether autophagy receptors/adaptors that contribute to selective autophagy but also regulate endosome and autophagosome maturation might play a role. Surprisingly, although these receptors share a high structural homology and similar functions, we identified a single autophagy adaptor that strongly influences the presentation of viral antigens by MHC-II molecules. Although silencing of this autophagy adaptor does not impact the expression levels and the recycling of MHC-II molecules, it has a major influence on the ligandome of MHC-II molecules. In the absence of this adaptor, MHC-II molecules accumulate at the proximity of the nucleus in CD63+Lamp1+ acidified compartments. In addition, the lack of this autophagy adaptor has a strong influence on the invariant chain degradation and expression levels, strongly suggesting that it regulates the activation or traffic of vesicles involved in the processing of newly synthesised antigens. Interestingly, some viruses target these autophagy adaptors to favour viral replication. Our work might reveal new escape mechanisms developed by viruses to damper MHC-II restricted antigen presentation and immune responses.
Keywords	HIV infections ; RNA ; antigen presentation ; autophagosomes ; epitopes ; macroautophagy ; peptides ; traffic ; virus replication
Language	English
Dates of publication	2022-10
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2022.05.068
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Cologne/Königswinter

Zs.A 166: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Herpesviruses and autophagy: catch me if you can!

Cavignac, Yolaine / Esclatine, Audrey

Viruses

2010 Volume 2, Issue 1, Page(s) 314–333

Abstract: Autophagy is an evolutionarily conserved cellular degradation pathway involving the digestion of intracellular components via the lysosomal pathway. The autophagic pathway constitutively maintains cellular homeostasis by recycling cytoplasmic organelles ... ...

Abstract	Autophagy is an evolutionarily conserved cellular degradation pathway involving the digestion of intracellular components via the lysosomal pathway. The autophagic pathway constitutively maintains cellular homeostasis by recycling cytoplasmic organelles and proteins, but it is also stimulated by environmental stress conditions, such as starvation, oxidative stress, and the accumulation of misfolded proteins. It also acts as a cellular defense mechanism against microorganisms by contributing to both the innate and adaptive immunity, and by eliminating intracellular pathogens (xenophagy). There is growing evidence that host cells try to control Herpesvirus infections by activating the autophagic machinery. However, it is well-known that Herpesviruses are smart pathogens and several, such as HSV-1, HCMV and HHV-8, are known to have developed numerous defense strategies for evading the host's immune response. Inhibition of the antiviral autophagic mechanism has also been reported. Autophagy has also been shown to enhance the major histocompatibility complex presentation of at least two viral proteins, the EBV-encoded EBNA-1 and the HSV-1 encoded gB. In this review, we present an overview of recent advances in our understanding of the complex interplay between autophagy and Herpesviruses.
Language	English
Publishing date	2010-01-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v2010314
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito