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Article ; Online: Temporal-iCLIP captures co-transcriptional RNA-protein interactions.

Cordiner, Ross A / Dou, Yuhui / Thomsen, Rune / Bugai, Andrii / Granneman, Sander / Heick Jensen, Torben

2023 Volume 14, Issue 1, Page(s) 696

Abstract: Dynamic RNA-protein interactions govern the co-transcriptional packaging of RNA polymerase II (RNAPII)-derived transcripts. Yet, our current understanding of this process in vivo primarily stems from steady state analysis. To remedy this, we here conduct ...

Abstract	Dynamic RNA-protein interactions govern the co-transcriptional packaging of RNA polymerase II (RNAPII)-derived transcripts. Yet, our current understanding of this process in vivo primarily stems from steady state analysis. To remedy this, we here conduct temporal-iCLIP (tiCLIP), combining RNAPII transcriptional synchronisation with UV cross-linking of RNA-protein complexes at serial timepoints. We apply tiCLIP to the RNA export adaptor, ALYREF; a component of the Nuclear Exosome Targeting (NEXT) complex, RBM7; and the nuclear cap binding complex (CBC). Regardless of function, all tested factors interact with nascent RNA as it exits RNAPII. Moreover, we demonstrate that the two transesterification steps of pre-mRNA splicing temporally separate ALYREF and RBM7 binding to splicing intermediates, and that exon-exon junction density drives RNA 5'end binding of ALYREF. Finally, we identify underappreciated steps in snoRNA 3'end processing performed by RBM7. Altogether, our data provide a temporal view of RNA-protein interactions during the early phases of transcription.
MeSH term(s)	RNA-Binding Proteins/metabolism ; Cell Nucleus/metabolism ; RNA Precursors/metabolism ; RNA Splicing ; RNA Polymerase II/metabolism ; RNA, Small Nucleolar/metabolism
Chemical Substances	RNA-Binding Proteins ; RNA Precursors ; RNA Polymerase II (EC 2.7.7.-) ; RNA, Small Nucleolar
Language	English
Publishing date	2023-02-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-36345-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: P-TEFb promotes cell survival upon p53 activation by suppressing intrinsic apoptosis pathway.

Wang, Zhijia / Mačáková, Monika / Bugai, Andrii / Kuznetsov, Sergey G / Hassinen, Antti / Lenasi, Tina / Potdar, Swapnil / Friedel, Caroline C / Barborič, Matjaž

Nucleic acids research

2023 Volume 51, Issue 4, Page(s) 1687–1706

Abstract: Positive transcription elongation factor b (P-TEFb) is the crucial player in RNA polymerase II (Pol II) pause release that has emerged as a promising target in cancer. Because single-agent therapy may fail to deliver durable clinical response, targeting ... ...

Abstract	Positive transcription elongation factor b (P-TEFb) is the crucial player in RNA polymerase II (Pol II) pause release that has emerged as a promising target in cancer. Because single-agent therapy may fail to deliver durable clinical response, targeting of P-TEFb shall benefit when deployed as a combination therapy. We screened a comprehensive oncology library and identified clinically relevant antimetabolites and Mouse double minute 2 homolog (MDM2) inhibitors as top compounds eliciting p53-dependent death of colorectal cancer cells in synergy with selective inhibitors of P-TEFb. While the targeting of P-TEFb augments apoptosis by anti-metabolite 5-fluorouracil, it switches the fate of cancer cells by the non-genotoxic MDM2 inhibitor Nutlin-3a from cell-cycle arrest to apoptosis. Mechanistically, the fate switching is enabled by the induction of p53-dependent pro-apoptotic genes and repression of P-TEFb-dependent pro-survival genes of the PI3K-AKT signaling cascade, which stimulates caspase 9 and intrinsic apoptosis pathway in BAX/BAK-dependent manner. Finally, combination treatments trigger apoptosis of cancer cell spheroids. Together, co-targeting of P-TEFb and suppressors of intrinsic apoptosis could become a viable strategy to eliminate cancer cells.
MeSH term(s)	Apoptosis ; Cell Line, Tumor ; Cell Survival ; Phosphatidylinositol 3-Kinases/metabolism ; Positive Transcriptional Elongation Factor B/antagonists & inhibitors ; Positive Transcriptional Elongation Factor B/metabolism ; Proto-Oncogene Proteins c-mdm2/genetics ; Tumor Suppressor Protein p53/genetics ; Humans
Chemical Substances	Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Positive Transcriptional Elongation Factor B (EC 2.7.11.-) ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27) ; Tumor Suppressor Protein p53 ; MDM2 protein, human (EC 2.3.2.27)
Language	English
Publishing date	2023-02-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkad001
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Article ; Online: Cracking the control of RNA polymerase II elongation by 7SK snRNP and P-TEFb.

C Quaresma, Alexandre J / Bugai, Andrii / Barboric, Matjaz

Nucleic acids research

2016 Volume 44, Issue 16, Page(s) 7527–7539

Abstract: Release of RNA polymerase II (Pol II) from promoter-proximal pausing has emerged as a critical step regulating gene expression in multicellular organisms. The transition of Pol II into productive elongation requires the kinase activity of positive ... ...

Abstract	Release of RNA polymerase II (Pol II) from promoter-proximal pausing has emerged as a critical step regulating gene expression in multicellular organisms. The transition of Pol II into productive elongation requires the kinase activity of positive transcription elongation factor b (P-TEFb), which is itself under a stringent control by the inhibitory 7SK small nuclear ribonucleoprotein (7SK snRNP) complex. Here, we provide an overview on stimulating Pol II pause release by P-TEFb and on sequestering P-TEFb into 7SK snRNP. Furthermore, we highlight mechanisms that govern anchoring of 7SK snRNP to chromatin as well as means that release P-TEFb from the inhibitory complex, and propose a unifying model of P-TEFb activation on chromatin. Collectively, these studies shine a spotlight on the central role of RNA binding proteins (RBPs) in directing the inhibition and activation of P-TEFb, providing a compelling paradigm for controlling Pol II transcription with a non-coding RNA.
MeSH term(s)	Animals ; Chromatin/metabolism ; Humans ; Models, Biological ; Positive Transcriptional Elongation Factor B/metabolism ; RNA Polymerase II/metabolism ; Ribonucleoproteins, Small Nuclear/metabolism ; Transcription Elongation, Genetic
Chemical Substances	Chromatin ; Ribonucleoproteins, Small Nuclear ; Positive Transcriptional Elongation Factor B (EC 2.7.11.-) ; RNA Polymerase II (EC 2.7.7.-)
Language	English
Publishing date	2016-09-19
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkw585
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Article ; Online: ARS2 instructs early transcription termination-coupled RNA decay by recruiting ZC3H4 to nascent transcripts.

Rouvière, Jérôme O / Salerno-Kochan, Anna / Lykke-Andersen, Søren / Garland, William / Dou, Yuhui / Rathore, Om / Molska, Ewa Šmidová / Wu, Guifen / Schmid, Manfred / Bugai, Andrii / Jakobsen, Lis / Žumer, Kristina / Cramer, Patrick / Andersen, Jens S / Conti, Elena / Jensen, Torben Heick

Molecular cell

2023 Volume 83, Issue 13, Page(s) 2240–2257.e6

Abstract: The RNA-binding ARS2 protein is centrally involved in both early RNA polymerase II (RNAPII) transcription termination and transcript decay. Despite its essential nature, the mechanisms by which ARS2 enacts these functions have remained unclear. Here, we ... ...

Abstract	The RNA-binding ARS2 protein is centrally involved in both early RNA polymerase II (RNAPII) transcription termination and transcript decay. Despite its essential nature, the mechanisms by which ARS2 enacts these functions have remained unclear. Here, we show that a conserved basic domain of ARS2 binds a corresponding acidic-rich, short linear motif (SLiM) in the transcription restriction factor ZC3H4. This interaction recruits ZC3H4 to chromatin to elicit RNAPII termination, independent of other early termination pathways defined by the cleavage and polyadenylation (CPA) and Integrator (INT) complexes. We find that ZC3H4, in turn, forms a direct connection to the nuclear exosome targeting (NEXT) complex, hereby facilitating rapid degradation of the nascent RNA. Hence, ARS2 instructs the coupled transcription termination and degradation of the transcript onto which it is bound. This contrasts with ARS2 function at CPA-instructed termination sites where the protein exclusively partakes in RNA suppression via post-transcriptional decay.
MeSH term(s)	Nuclear Proteins/metabolism ; Transcription, Genetic ; Transcription Factors/metabolism ; RNA Polymerase II/genetics ; RNA Polymerase II/metabolism ; RNA Stability/genetics ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; RNA
Chemical Substances	Nuclear Proteins ; Transcription Factors ; RNA Polymerase II (EC 2.7.7.-) ; RNA-Binding Proteins ; RNA (63231-63-0)
Language	English
Publishing date	2023-06-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2023.05.028
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Article ; Online: P-TEFb Activation by RBM7 Shapes a Pro-survival Transcriptional Response to Genotoxic Stress.

Bugai, Andrii / Quaresma, Alexandre J C / Friedel, Caroline C / Lenasi, Tina / Düster, Robert / Sibley, Christopher R / Fujinaga, Koh / Kukanja, Petra / Hennig, Thomas / Blasius, Melanie / Geyer, Matthias / Ule, Jernej / Dölken, Lars / Barborič, Matjaž

Molecular cell

2019 Volume 74, Issue 2, Page(s) 254–267.e10

Abstract: DNA damage response (DDR) involves dramatic transcriptional alterations, the mechanisms of which remain ill defined. Here, we show that following genotoxic stress, the RNA-binding motif protein 7 (RBM7) stimulates RNA polymerase II (Pol II) transcription ...

Abstract	DNA damage response (DDR) involves dramatic transcriptional alterations, the mechanisms of which remain ill defined. Here, we show that following genotoxic stress, the RNA-binding motif protein 7 (RBM7) stimulates RNA polymerase II (Pol II) transcription and promotes cell viability by activating the positive transcription elongation factor b (P-TEFb) via its release from the inhibitory 7SK small nuclear ribonucleoprotein (7SK snRNP). This is mediated by activation of p38
MeSH term(s)	Apoptosis/genetics ; Cell Survival/genetics ; DNA Damage/genetics ; HEK293 Cells ; Humans ; Positive Transcriptional Elongation Factor B/genetics ; RNA Polymerase II/genetics ; RNA, Long Noncoding/genetics ; RNA-Binding Proteins/genetics ; Ribonucleoproteins, Small Nuclear/genetics ; Transcription, Genetic ; p38 Mitogen-Activated Protein Kinases/genetics
Chemical Substances	RBM7 protein, human ; RNA, Long Noncoding ; RNA-Binding Proteins ; Ribonucleoproteins, Small Nuclear ; long non-coding RNA 7SK, human ; Positive Transcriptional Elongation Factor B (EC 2.7.11.-) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; RNA Polymerase II (EC 2.7.7.-)
Language	English
Publishing date	2019-02-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2019.01.033
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Article: P-TEFb Activation by RBM7 Shapes a Pro-survival Transcriptional Response to Genotoxic Stress

Bugai, Andrii / Quaresma, Alexandre J.C / Friedel, Caroline C / Lenasi, Tina / Düster, Robert / Sibley, Christopher R / Fujinaga, Koh / Kukanja, Petra / Hennig, Thomas / Blasius, Melanie / Geyer, Matthias / Ule, Jernej / Dölken, Lars / Barborič, Matjaž

Molecular cell. 2019 Apr. 18, v. 74, no. 2

2019

Abstract	DNA damage response (DDR) involves dramatic transcriptional alterations, the mechanisms of which remain ill defined. Here, we show that following genotoxic stress, the RNA-binding motif protein 7 (RBM7) stimulates RNA polymerase II (Pol II) transcription and promotes cell viability by activating the positive transcription elongation factor b (P-TEFb) via its release from the inhibitory 7SK small nuclear ribonucleoprotein (7SK snRNP). This is mediated by activation of p38MAPK, which triggers enhanced binding of RBM7 with core subunits of 7SK snRNP. In turn, P-TEFb relocates to chromatin to induce transcription of short units, including key DDR genes and multiple classes of non-coding RNAs. Critically, interfering with the axis of RBM7 and P-TEFb provokes cellular hypersensitivity to DNA-damage-inducing agents due to activation of apoptosis. Our work uncovers the importance of stress-dependent stimulation of Pol II pause release, which enables a pro-survival transcriptional response that is crucial for cell fate upon genotoxic insult.
Keywords	DNA damage ; DNA-directed RNA polymerase ; apoptosis ; cell viability ; chromatin ; genes ; mutagens ; non-coding RNA ; ribonucleoproteins ; transcription (genetics) ; transcriptional elongation factors
Language	English
Dates of publication	2019-0418
Size	p. 254-267.e10.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2019.01.033
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Article: Chemical, Physical and Biological Triggers of Evolutionary Conserved Bcl-xL-Mediated Apoptosis.

Ianevski, Aleksandr / Kulesskiy, Evgeny / Krpina, Klara / Lou, Guofeng / Aman, Yahyah / Bugai, Andrii / Aasumets, Koit / Akimov, Yevhen / Bulanova, Daria / Gildemann, Kiira / Arutyunyan, Albert F / Susova, Olga Yu / Zhuze, Alexei L / Ji, Ping / Wang, Wei / Holien, Toril / Bugge, Marit / Zusinaite, Eva / Oksenych, Valentyn /

Lysvand, Hilde / Gerhold, Joachim M / Bjørås, Magnar / Johansen, Pål / Waage, Anders / Heckman, Caroline A / Fang, Evandro F / Kainov, Denis E

Cancers

2020 Volume 12, Issue 6

Abstract: Background: The evidence that pan-Bcl-2 or Bcl-xL-specific inhibitors prematurely kill virus-infected or RNA/DNA-transfected cells provides rationale for investigating these apoptotic inducers further. We hypothesized that not only invasive RNA or DNA ( ... ...

Abstract	Background: The evidence that pan-Bcl-2 or Bcl-xL-specific inhibitors prematurely kill virus-infected or RNA/DNA-transfected cells provides rationale for investigating these apoptotic inducers further. We hypothesized that not only invasive RNA or DNA (biological factors) but also DNA/RNA-damaging chemical or physical factors could trigger apoptosis that have been sensitized with pan-Bcl-2 or Bcl-xL-specific agents; Methods: We tested chemical and physical factors plus Bcl-xL-specific inhibitor A-1155463 in cells of various origins and the small roundworms (
Language	English
Publishing date	2020-06-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers12061694
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Article: Influenza virus NS1 protein binds cellular DNA to block transcription of antiviral genes.

Anastasina, Maria / Le May, Nicolas / Bugai, Andrii / Fu, Yu / Söderholm, Sandra / Gaelings, Lana / Ohman, Tiina / Tynell, Janne / Kyttänen, Suvi / Barboric, Matjaz / Nyman, Tuula A / Matikainen, Sampsa / Julkunen, Ilkka / Butcher, Sarah J / Egly, Jean-Marc / Kainov, Denis E

Biochimica et biophysica acta

2016 Volume 1859, Issue 11, Page(s) 1440–1448

Abstract: Influenza NS1 protein is an important virulence factor that is capable of binding double-stranded (ds) RNA and inhibiting dsRNA-mediated host innate immune responses. Here we show that NS1 can also bind cellular dsDNA. This interaction prevents loading ... ...

Abstract	Influenza NS1 protein is an important virulence factor that is capable of binding double-stranded (ds) RNA and inhibiting dsRNA-mediated host innate immune responses. Here we show that NS1 can also bind cellular dsDNA. This interaction prevents loading of transcriptional machinery to the DNA, thereby attenuating IAV-mediated expression of antiviral genes. Thus, we identified a previously undescribed strategy, by which RNA virus inhibits cellular transcription to escape antiviral response and secure its replication.
MeSH term(s)	Animals ; Cell Line ; Chromatin/metabolism ; DNA/metabolism ; Humans ; Influenza A virus/physiology ; Protein Binding ; Transcription, Genetic/physiology ; Viral Nonstructural Proteins/metabolism ; Viral Nonstructural Proteins/physiology ; Virus Replication
Chemical Substances	Chromatin ; INS1 protein, influenza virus ; Viral Nonstructural Proteins ; DNA (9007-49-2)
Language	English
Publishing date	2016
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagrm.2016.09.005
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Article ; Online: Regulation of kynurenine biosynthesis during influenza virus infection.

The FEBS journal

2016 Volume 284, Issue 2, Page(s) 222–236

Abstract: Influenza A viruses (IAVs) remain serious threats to public health because of the shortage of effective means of control. Developing more effective virus control modalities requires better understanding of virus-host interactions. It has previously been ... ...

Abstract	Influenza A viruses (IAVs) remain serious threats to public health because of the shortage of effective means of control. Developing more effective virus control modalities requires better understanding of virus-host interactions. It has previously been shown that IAV induces the production of kynurenine, which suppresses T-cell responses, enhances pain hypersensitivity and disturbs behaviour in infected animals. However, the regulation of kynurenine biosynthesis during IAV infection remains elusive. Here we showed that IAV infection induced expression of interferons (IFNs), which upregulated production of indoleamine-2,3-dioxygenase (IDO1), which catalysed the kynurenine biosynthesis. Furthermore, IAV attenuated the IDO1 expression and the production of kynurenine through its NS1 protein. Interestingly, inhibition of viral replication prior to IFN induction limited IDO1 expression, while inhibition after did not. Finally, we showed that kynurenine biosynthesis was activated in macrophages in response to other stimuli, such as influenza B virus, herpes simplex virus 1 and 2 as well as bacterial lipopolysaccharides. Thus, the tight regulation of the kynurenine biosynthesis by host cell and, perhaps, pathogen might be a basic signature of a wide range of host-pathogen interactions, which should be taken into account during development of novel antiviral and antibacterial drugs.
MeSH term(s)	Animals ; Antiviral Agents/pharmacology ; Female ; Gene Expression Regulation ; Host-Pathogen Interactions ; Humans ; Immunologic Factors/pharmacology ; Indoleamine-Pyrrole 2,3,-Dioxygenase/antagonists & inhibitors ; Indoleamine-Pyrrole 2,3,-Dioxygenase/genetics ; Indoleamine-Pyrrole 2,3,-Dioxygenase/immunology ; Influenza A Virus, H1N1 Subtype/drug effects ; Influenza A Virus, H1N1 Subtype/genetics ; Influenza A Virus, H1N1 Subtype/growth & development ; Influenza A Virus, H1N1 Subtype/metabolism ; Interferons/genetics ; Interferons/immunology ; Kynurenine/antagonists & inhibitors ; Kynurenine/biosynthesis ; Lung/drug effects ; Lung/immunology ; Lung/virology ; Macrophages/drug effects ; Macrophages/virology ; Metabolic Networks and Pathways/drug effects ; Metabolic Networks and Pathways/genetics ; Metabolic Networks and Pathways/immunology ; Mice ; Mice, Inbred BALB C ; Orthomyxoviridae Infections/drug therapy ; Orthomyxoviridae Infections/immunology ; Orthomyxoviridae Infections/pathology ; Orthomyxoviridae Infections/virology ; Oxazoles/pharmacology ; Oximes/pharmacology ; Primary Cell Culture ; Pyrroles/pharmacology ; Sulfonamides/pharmacology ; Thiazoles/pharmacology ; Transcriptome ; Tryptophan/metabolism ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Virus Replication
Chemical Substances	Antiviral Agents ; IDO1 protein, human ; INS1 protein, influenza virus ; Immunologic Factors ; Indoleamine-Pyrrole 2,3,-Dioxygenase ; N-(5-(((5-(1,1-dimethylethyl)-2-oxazolyl)methyl)thio)-2-thiazolyl)-4-piperidinecarboxamide ; Oxazoles ; Oximes ; Pyrroles ; Sulfonamides ; Thiazoles ; Viral Nonstructural Proteins ; Kynurenine (343-65-7) ; epacadostat (71596A9R13) ; Tryptophan (8DUH1N11BX) ; Interferons (9008-11-1) ; obatoclax (QN4128B52A)
Language	English
Publishing date	2016-12-14
Publishing country	England
Document type	Editorial
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13966
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Article ; Online: Antiviral Properties of Chemical Inhibitors of Cellular Anti-Apoptotic Bcl-2 Proteins.

Bulanova, Daria / Ianevski, Aleksandr / Bugai, Andrii / Akimov, Yevhen / Kuivanen, Suvi / Paavilainen, Henrik / Kakkola, Laura / Nandania, Jatin / Turunen, Laura / Ohman, Tiina / Ala-Hongisto, Hanna / Pesonen, Hanna M / Kuisma, Marika S / Honkimaa, Anni / Walton, Emma L / Oksenych, Valentyn / Lorey, Martina B / Guschin, Dmitry / Shim, Jungmin /

Viruses

2017 Volume 9, Issue 10

Abstract: Viral diseases remain serious threats to public health because of the shortage of effective means of control. To combat the surge of viral diseases, new treatments are urgently needed. Here we show that small-molecules, which inhibit cellular anti- ... ...

Abstract	Viral diseases remain serious threats to public health because of the shortage of effective means of control. To combat the surge of viral diseases, new treatments are urgently needed. Here we show that small-molecules, which inhibit cellular anti-apoptotic Bcl-2 proteins (Bcl-2i), induced the premature death of cells infected with different RNA or DNA viruses, whereas, at the same concentrations, no toxicity was observed in mock-infected cells. Moreover, these compounds limited viral replication and spread. Surprisingly, Bcl-2i also induced the premature apoptosis of cells transfected with viral RNA or plasmid DNA but not of mock-transfected cells. These results suggest that Bcl-2i sensitizes cells containing foreign RNA or DNA to apoptosis. A comparison of the toxicity, antiviral activity, and side effects of six Bcl-2i allowed us to select A-1155463 as an antiviral lead candidate. Thus, our results pave the way for the further development of Bcl-2i for the prevention and treatment of viral diseases.
Keywords	covid19
Language	English
Publishing date	2017-09-25
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/v9100271
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