LIVIVO - Search results -

Search results

Result 1 - 8 of total 8

Search options

Article ; Online: Histone acetylation in neuronal (dys)function.

Bonnaud, Emilie M / Suberbielle, Elsa / Malnou, Cécile E

2016 Volume 7, Issue 2, Page(s) 103–116

Abstract: Cognitive functions require the expression of an appropriate pattern of genes in response to environmental stimuli. Over the last years, many studies have accumulated knowledge towards the understanding of molecular mechanisms that regulate neuronal gene ...

Abstract	Cognitive functions require the expression of an appropriate pattern of genes in response to environmental stimuli. Over the last years, many studies have accumulated knowledge towards the understanding of molecular mechanisms that regulate neuronal gene expression. Epigenetic modifications have been shown to play an important role in numerous neuronal functions, from synaptic plasticity to learning and memory. In particular, histone acetylation is a central player in these processes. In this review, we present the molecular mechanisms of histone acetylation and summarize the data underlying the relevance of histone acetylation in cognitive functions in normal and pathological conditions. In the last part, we discuss the different mechanisms underlying the dysregulation of histone acetylation associated with neurological disorders, with a particular focus on environmental causes (stress, drugs, or infectious agents) that are linked to impaired histone acetylation.
MeSH term(s)	Acetylation ; Animals ; Cognition ; Environment ; Epigenesis, Genetic ; Gene Expression Regulation ; Genetic Predisposition to Disease ; Histones/metabolism ; Humans ; Memory ; Mutation ; Neurodegenerative Diseases/etiology ; Neurodegenerative Diseases/metabolism ; Neuronal Plasticity ; Neurons/physiology
Chemical Substances	Histones
Language	English
Publishing date	2016-05-01
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	2557908-3
ISSN	1868-503X ; 1868-5021
ISSN (online)	1868-503X
ISSN	1868-5021
DOI	10.1515/bmc-2016-0002
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 7056: 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: Histone acetylation in neuronal (dys)function

Bonnaud Emilie M. / Suberbielle Elsa / Malnou Cécile E.

Biomolecular Concepts, Vol 7, Iss 2, Pp 103-

2016 Volume 116

Abstract	Cognitive functions require the expression of an appropriate pattern of genes in response to environmental stimuli. Over the last years, many studies have accumulated knowledge towards the understanding of molecular mechanisms that regulate neuronal gene expression. Epigenetic modifications have been shown to play an important role in numerous neuronal functions, from synaptic plasticity to learning and memory. In particular, histone acetylation is a central player in these processes. In this review, we present the molecular mechanisms of histone acetylation and summarize the data underlying the relevance of histone acetylation in cognitive functions in normal and pathological conditions. In the last part, we discuss the different mechanisms underlying the dysregulation of histone acetylation associated with neurological disorders, with a particular focus on environmental causes (stress, drugs, or infectious agents) that are linked to impaired histone acetylation.
Keywords	cognition ; epigenetics ; histone acetylation ; histone acetyltransferase ; histone deacetylase ; neuron ; synaptic plasticity ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2016-05-01T00:00:00Z
Publisher	De Gruyter
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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: Comparison of intra- and inter-host genetic diversity in rabies virus during experimental cross-species transmission.

Bonnaud, Emilie M / Troupin, Cécile / Dacheux, Laurent / Holmes, Edward C / Monchatre-Leroy, Elodie / Tanguy, Marion / Bouchier, Christiane / Cliquet, Florence / Barrat, Jacques / Bourhy, Hervé

PLoS pathogens

2019 Volume 15, Issue 6, Page(s) e1007799

Abstract: The development of high-throughput genome sequencing enables accurate measurements of levels of sub-consensus intra-host virus genetic diversity and analysis of the role played by natural selection during cross-species transmission. We analysed the ... ...

Abstract	The development of high-throughput genome sequencing enables accurate measurements of levels of sub-consensus intra-host virus genetic diversity and analysis of the role played by natural selection during cross-species transmission. We analysed the natural and experimental evolution of rabies virus (RABV), an important example of a virus that is able to make multiple host jumps. In particular, we (i) analyzed RABV evolution during experimental host switching with the goal of identifying possible genetic markers of host adaptation, (ii) compared the mutational changes observed during passage with those observed in natura, and (iii) determined whether the colonization of new hosts or tissues requires adaptive evolution in the virus. To address these aims, animal infection models (dog and fox) and primary cell culture models (embryo brain cells of dog and fox) were developed and viral variation was studied in detail through deep genome sequencing. Our analysis revealed a strong unidirectional host evolutionary effect, as dog-adapted rabies virus was able to replicate in fox and fox cells relatively easily, while dogs or neuronal dog cells were not easily susceptible to fox adapted-RABV. This suggests that dog RABV may be able to adapt to some hosts more easily than other host variants, or that when RABV switched from dogs to red foxes it lost its ability to adapt easily to other species. Although no difference in patterns of mutation variation between different host organs was observed, mutations were common following both in vitro and in vivo passage. However, only a small number of these mutations also appeared in natura, suggesting that adaptation during successful cross-species virus transmission is a complex, multifactorial evolutionary process.
MeSH term(s)	Animals ; Cell Line ; Dog Diseases/genetics ; Dog Diseases/immunology ; Dogs ; Evolution, Molecular ; Female ; Foxes/genetics ; Foxes/immunology ; Foxes/virology ; High-Throughput Nucleotide Sequencing ; Host-Parasite Interactions/genetics ; Host-Parasite Interactions/immunology ; Male ; Mutation ; Rabies/genetics ; Rabies/immunology ; Rabies virus/physiology
Language	English
Publishing date	2019-06-20
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.1007799
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Hippocampal expression of a virus-derived protein impairs memory in mice.

Bétourné, Alexandre / Szelechowski, Marion / Thouard, Anne / Abrial, Erika / Jean, Arnaud / Zaidi, Falek / Foret, Charlotte / Bonnaud, Emilie M / Charlier, Caroline M / Suberbielle, Elsa / Malnou, Cécile E / Granon, Sylvie / Rampon, Claire / Gonzalez-Dunia, Daniel

Proceedings of the National Academy of Sciences of the United States of America

2018 Volume 115, Issue 7, Page(s) 1611–1616

Abstract: The analysis of the biology of neurotropic viruses, notably of their interference with cellular signaling, provides a useful tool to get further insight into the role of specific pathways in the control of behavioral functions. Here, we exploited the ... ...

Abstract	The analysis of the biology of neurotropic viruses, notably of their interference with cellular signaling, provides a useful tool to get further insight into the role of specific pathways in the control of behavioral functions. Here, we exploited the natural property of a viral protein identified as a major effector of behavioral disorders during infection. We used the phosphoprotein (P) of Borna disease virus, which acts as a decoy substrate for protein kinase C (PKC) when expressed in neurons and disrupts synaptic plasticity. By a lentiviral-based strategy, we directed the singled-out expression of P in the dentate gyrus of the hippocampus and we examined its impact on mouse behavior. Mice expressing the P protein displayed increased anxiety and impaired long-term memory in contextual and spatial memory tasks. Interestingly, these effects were dependent on P protein phosphorylation by PKC, as expression of a mutant form of P devoid of its PKC phosphorylation sites had no effect on these behaviors. We also revealed features of behavioral impairment induced by P protein expression but that were independent of its phosphorylation by PKC. Altogether, our findings provide insight into the behavioral correlates of viral infection, as well as into the impact of virus-mediated alterations of the PKC pathway on behavioral functions.
MeSH term(s)	Animals ; Borna Disease/metabolism ; Borna Disease/pathology ; Borna Disease/virology ; Borna disease virus/physiology ; Cells, Cultured ; Cognition Disorders/etiology ; Cognition Disorders/metabolism ; Cognition Disorders/pathology ; Dentate Gyrus/metabolism ; Dentate Gyrus/pathology ; Dentate Gyrus/virology ; Hippocampus/metabolism ; Hippocampus/pathology ; Hippocampus/virology ; Memory, Long-Term/physiology ; Mice ; Mutation ; Neuronal Plasticity ; Neurons/metabolism ; Neurons/pathology ; Neurons/virology ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; Viral Structural Proteins/genetics ; Viral Structural Proteins/metabolism
Chemical Substances	P protein, Borna disease virus ; Phosphoproteins ; Viral Structural Proteins ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2018--13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1711977115
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: 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: Comparison of intra- and inter-host genetic diversity in rabies virus during experimental cross-species transmission.

Emilie M Bonnaud / Cécile Troupin / Laurent Dacheux / Edward C Holmes / Elodie Monchatre-Leroy / Marion Tanguy / Christiane Bouchier / Florence Cliquet / Jacques Barrat / Hervé Bourhy

PLoS Pathogens, Vol 15, Iss 6, p e

2019 Volume 1007799

Abstract	The development of high-throughput genome sequencing enables accurate measurements of levels of sub-consensus intra-host virus genetic diversity and analysis of the role played by natural selection during cross-species transmission. We analysed the natural and experimental evolution of rabies virus (RABV), an important example of a virus that is able to make multiple host jumps. In particular, we (i) analyzed RABV evolution during experimental host switching with the goal of identifying possible genetic markers of host adaptation, (ii) compared the mutational changes observed during passage with those observed in natura, and (iii) determined whether the colonization of new hosts or tissues requires adaptive evolution in the virus. To address these aims, animal infection models (dog and fox) and primary cell culture models (embryo brain cells of dog and fox) were developed and viral variation was studied in detail through deep genome sequencing. Our analysis revealed a strong unidirectional host evolutionary effect, as dog-adapted rabies virus was able to replicate in fox and fox cells relatively easily, while dogs or neuronal dog cells were not easily susceptible to fox adapted-RABV. This suggests that dog RABV may be able to adapt to some hosts more easily than other host variants, or that when RABV switched from dogs to red foxes it lost its ability to adapt easily to other species. Although no difference in patterns of mutation variation between different host organs was observed, mutations were common following both in vitro and in vivo passage. However, only a small number of these mutations also appeared in natura, suggesting that adaptation during successful cross-species virus transmission is a complex, multifactorial evolutionary process.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Subject code	630
Language	English
Publishing date	2019-06-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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: Borna disease virus phosphoprotein modulates epigenetic signaling in neurons to control viral replication.

Bonnaud, Emilie M / Szelechowski, Marion / Bétourné, Alexandre / Foret, Charlotte / Thouard, Anne / Gonzalez-Dunia, Daniel / Malnou, Cécile E

Journal of virology

2015 Volume 89, Issue 11, Page(s) 5996–6008

Abstract: Unlabelled: Understanding the modalities of interaction of neurotropic viruses with their target cells represents a major challenge that may improve our knowledge of many human neurological disorders for which viral origin is suspected. Borna disease ... ...

Abstract	Unlabelled: Understanding the modalities of interaction of neurotropic viruses with their target cells represents a major challenge that may improve our knowledge of many human neurological disorders for which viral origin is suspected. Borna disease virus (BDV) represents an ideal model to analyze the molecular mechanisms of viral persistence in neurons and its consequences for neuronal homeostasis. It is now established that BDV ensures its long-term maintenance in infected cells through a stable interaction of viral components with the host cell chromatin, in particular, with core histones. This has led to our hypothesis that such an interaction may trigger epigenetic changes in the host cell. Here, we focused on histone acetylation, which plays key roles in epigenetic regulation of gene expression, notably for neurons. We performed a comparative analysis of histone acetylation patterns of neurons infected or not infected by BDV, which revealed that infection decreases histone acetylation on selected lysine residues. We showed that the BDV phosphoprotein (P) is responsible for these perturbations, even when it is expressed alone independently of the viral context, and that this action depends on its phosphorylation by protein kinase C. We also demonstrated that BDV P inhibits cellular histone acetyltransferase activities. Finally, by pharmacologically manipulating cellular acetylation levels, we observed that inhibiting cellular acetyl transferases reduces viral replication in cell culture. Our findings reveal that manipulation of cellular epigenetics by BDV could be a means to modulate viral replication and thus illustrate a fascinating example of virus-host cell interaction. Importance: Persistent DNA viruses often subvert the mechanisms that regulate cellular chromatin dynamics, thereby benefitting from the resulting epigenetic changes to create a favorable milieu for their latent and persistent states. Here, we reasoned that Borna disease virus (BDV), the only RNA virus known to durably persist in the nucleus of infected cells, notably neurons, might employ a similar mechanism. In this study, we uncovered a novel modality of virus-cell interaction in which BDV phosphoprotein inhibits cellular histone acetylation by interfering with histone acetyltransferase activities. Manipulation of cellular histone acetylation is accompanied by a modulation of viral replication, revealing a perfect adaptation of this "ancient" virus to its host that may favor neuronal persistence and limit cellular damage.
MeSH term(s)	Acetylation ; Animals ; Borna disease virus/physiology ; Cells, Cultured ; Epigenesis, Genetic ; Histones/metabolism ; Host-Pathogen Interactions ; Neurons/virology ; Phosphoproteins/metabolism ; Protein Processing, Post-Translational ; Rats, Sprague-Dawley ; Viral Structural Proteins/metabolism ; Virus Replication
Chemical Substances	Histones ; P protein, Borna disease virus ; Phosphoproteins ; Viral Structural Proteins
Language	English
Publishing date	2015-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00454-15
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

In stock of ZB MED Cologne/Königswinter

Zs.A 609: 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 ▾

Article ; Online: Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway.

Sonthonnax, Florian / Besson, Benoit / Bonnaud, Emilie / Jouvion, Grégory / Merino, David / Larrous, Florence / Bourhy, Hervé

Scientific reports

2019 Volume 9, Issue 1, Page(s) 12171

Abstract: Phosphoprotein (P) and matrix protein (M) cooperate to undermine the immune response ... through the cytoplasmic retention of interferon (IFN)-activated STAT1 (pSTAT1), M interacts with the RelAp43-p105-ABIN2 ... protein-complementation assays, reverse genetics and DNA ChIP, we identified a role of M protein ...

Abstract	Phosphoprotein (P) and matrix protein (M) cooperate to undermine the immune response to rabies virus (RABV) infections. While P is involved in the modulation of the Jak-Stat pathway through the cytoplasmic retention of interferon (IFN)-activated STAT1 (pSTAT1), M interacts with the RelAp43-p105-ABIN2-TPL2 complex, to efficiently inhibit the nuclear factor-κB (NF-κB) pathway. Using transfections, protein-complementation assays, reverse genetics and DNA ChIP, we identified a role of M protein in the control of Jak-Stat signaling pathway, in synergy with the P protein. In unstimulated cells, both M and P proteins were found to interact with JAK1. Upon type-I IFN stimulation, the M switches toward pSTAT1 interaction, which results in an enhanced capacity of P protein to interact with pSTAT1 and restrain it in the cytoplasm. Furthermore, the role for M-protein positions 77, 100, 104 and 110 was also demonstrated in interaction with both JAK1 and pY-STAT1, and confirmed in vivo. Together, these data indicate that M protein cooperates with P protein to restrain in parallel, and sequentially, NF-κB and Jak-Stat pathways.
MeSH term(s)	Animals ; Cytoplasm/metabolism ; HeLa Cells ; Humans ; Immunity, Innate ; Interferon Type I/metabolism ; Janus Kinase 1/metabolism ; Lyssavirus/metabolism ; Lyssavirus/pathogenicity ; Mice ; Mice, Inbred BALB C ; Mutagenesis, Site-Directed ; NF-kappa B/metabolism ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Promoter Regions, Genetic ; STAT1 Transcription Factor/genetics ; STAT1 Transcription Factor/metabolism ; Signal Transduction ; Th2 Cells/immunology ; Th2 Cells/metabolism ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virulence
Chemical Substances	Interferon Type I ; NF-kappa B ; Phosphoproteins ; STAT1 Transcription Factor ; STAT1 protein, human ; Viral Matrix Proteins ; Viral Proteins ; JAK1 protein, human (EC 2.7.10.2) ; Janus Kinase 1 (EC 2.7.10.2)
Language	English
Publishing date	2019-08-21
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/s41598-019-48507-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway

Florian Sonthonnax / Benoit Besson / Emilie Bonnaud / Grégory Jouvion / David Merino / Florence Larrous / Hervé Bourhy

Scientific Reports, Vol 9, Iss 1, Pp 1-

2019 Volume 13

Abstract: Abstract Phosphoprotein (P) and matrix protein (M) cooperate to undermine the immune response ... through the cytoplasmic retention of interferon (IFN)-activated STAT1 (pSTAT1), M interacts with the RelAp43-p105-ABIN2 ... protein-complementation assays, reverse genetics and DNA ChIP, we identified a role of M protein ...

Abstract	Abstract Phosphoprotein (P) and matrix protein (M) cooperate to undermine the immune response to rabies virus (RABV) infections. While P is involved in the modulation of the Jak-Stat pathway through the cytoplasmic retention of interferon (IFN)-activated STAT1 (pSTAT1), M interacts with the RelAp43-p105-ABIN2-TPL2 complex, to efficiently inhibit the nuclear factor-κB (NF-κB) pathway. Using transfections, protein-complementation assays, reverse genetics and DNA ChIP, we identified a role of M protein in the control of Jak-Stat signaling pathway, in synergy with the P protein. In unstimulated cells, both M and P proteins were found to interact with JAK1. Upon type-I IFN stimulation, the M switches toward pSTAT1 interaction, which results in an enhanced capacity of P protein to interact with pSTAT1 and restrain it in the cytoplasm. Furthermore, the role for M-protein positions 77, 100, 104 and 110 was also demonstrated in interaction with both JAK1 and pY-STAT1, and confirmed in vivo. Together, these data indicate that M protein cooperates with P protein to restrain in parallel, and sequentially, NF-κB and Jak-Stat pathways.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2019-08-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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.

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

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

Full text online

More links

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED