The Antiviral Activities of Poly-ADP-Ribose Polymerases
The poly-adenosine diphosphate (ADP)-ribose polymerases (PARPs) are responsible for ADP-ribosylation, a reversible post-translational modification involved in many cellular processes including DNA damage repair, chromatin remodeling, regulation of translation and cell death. In addition to these phy...
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Format: | Article |
Language: | English |
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MDPI AG
2021-03-01
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Series: | Viruses |
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Online Access: | https://www.mdpi.com/1999-4915/13/4/582 |
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author | Mathilde Malgras Magali Garcia Clément Jousselin Charles Bodet Nicolas Lévêque |
author_facet | Mathilde Malgras Magali Garcia Clément Jousselin Charles Bodet Nicolas Lévêque |
author_sort | Mathilde Malgras |
collection | DOAJ |
description | The poly-adenosine diphosphate (ADP)-ribose polymerases (PARPs) are responsible for ADP-ribosylation, a reversible post-translational modification involved in many cellular processes including DNA damage repair, chromatin remodeling, regulation of translation and cell death. In addition to these physiological functions, recent studies have highlighted the role of PARPs in host defenses against viruses, either by direct antiviral activity, targeting certain steps of virus replication cycle, or indirect antiviral activity, via modulation of the innate immune response. This review focuses on the antiviral activity of PARPs, as well as strategies developed by viruses to escape their action. |
first_indexed | 2024-03-10T12:47:00Z |
format | Article |
id | doaj.art-f52704c218254e2397dd6bdd53fabee5 |
institution | Directory Open Access Journal |
issn | 1999-4915 |
language | English |
last_indexed | 2024-03-10T12:47:00Z |
publishDate | 2021-03-01 |
publisher | MDPI AG |
record_format | Article |
series | Viruses |
spelling | doaj.art-f52704c218254e2397dd6bdd53fabee52023-11-21T13:26:48ZengMDPI AGViruses1999-49152021-03-0113458210.3390/v13040582The Antiviral Activities of Poly-ADP-Ribose PolymerasesMathilde Malgras0Magali Garcia1Clément Jousselin2Charles Bodet3Nicolas Lévêque4Laboratoire Inflammation Tissus Epithéliaux et Cytokines, Université de Poitiers, 86073 Poitiers, FranceLaboratoire Inflammation Tissus Epithéliaux et Cytokines, Université de Poitiers, 86073 Poitiers, FranceLaboratoire Inflammation Tissus Epithéliaux et Cytokines, Université de Poitiers, 86073 Poitiers, FranceLaboratoire Inflammation Tissus Epithéliaux et Cytokines, Université de Poitiers, 86073 Poitiers, FranceLaboratoire Inflammation Tissus Epithéliaux et Cytokines, Université de Poitiers, 86073 Poitiers, FranceThe poly-adenosine diphosphate (ADP)-ribose polymerases (PARPs) are responsible for ADP-ribosylation, a reversible post-translational modification involved in many cellular processes including DNA damage repair, chromatin remodeling, regulation of translation and cell death. In addition to these physiological functions, recent studies have highlighted the role of PARPs in host defenses against viruses, either by direct antiviral activity, targeting certain steps of virus replication cycle, or indirect antiviral activity, via modulation of the innate immune response. This review focuses on the antiviral activity of PARPs, as well as strategies developed by viruses to escape their action.https://www.mdpi.com/1999-4915/13/4/582virusPARPantiviralimmunomodulationviral escape mechanisms |
spellingShingle | Mathilde Malgras Magali Garcia Clément Jousselin Charles Bodet Nicolas Lévêque The Antiviral Activities of Poly-ADP-Ribose Polymerases Viruses virus PARP antiviral immunomodulation viral escape mechanisms |
title | The Antiviral Activities of Poly-ADP-Ribose Polymerases |
title_full | The Antiviral Activities of Poly-ADP-Ribose Polymerases |
title_fullStr | The Antiviral Activities of Poly-ADP-Ribose Polymerases |
title_full_unstemmed | The Antiviral Activities of Poly-ADP-Ribose Polymerases |
title_short | The Antiviral Activities of Poly-ADP-Ribose Polymerases |
title_sort | antiviral activities of poly adp ribose polymerases |
topic | virus PARP antiviral immunomodulation viral escape mechanisms |
url | https://www.mdpi.com/1999-4915/13/4/582 |
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