Abstract
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.
Highlights
Poly-adenosine diphosphate (ADP)-ribose polymerases (PARPs) are a family of enzymes responsible for ADP-ribosylation, a reversible and transient post-translational modification of various target proteins including histones, enzymes, transcription factors and even PARPs themselves [1]
DNA-dependent PARPs act as DNA damage sensors involved in DNA break repair, with ADP-ribosylation at the double-stranded breaks acting as a signal, which allows the recruitment of DNA repair enzymes to the lesion site [11]
Cells enhances IFN-β mRNA expression and oligomerization of the viral RNA sensor retinoic acid-inducible gene I (RIG-I), which leads to robust activation of downstream antiviral signaling through the interferon regulatory factor 3 (IRF3) pathway [76]
Summary
Poly-adenosine diphosphate (ADP)-ribose polymerases (PARPs) are a family of enzymes responsible for ADP-ribosylation, a reversible and transient post-translational modification of various target proteins including histones, enzymes, transcription factors and even PARPs themselves [1]. DNA-dependent PARPs act as DNA damage sensors involved in DNA break repair, with ADP-ribosylation at the double-stranded breaks acting as a signal, which allows the recruitment of DNA repair enzymes to the lesion site [11]. DNA-dependent PARPs act as DNA damage sensors in of 14 volved in DNA break repair, with ADP-ribosylation at the double-stranded breaks acting as a signal, which allows the recruitment of DNA repair enzymes to the lesion site [11]. Every step of of thethe viral cycle, from entry intointo to exit fromfrom the infected cell, represents a potential target for for antiviral proteins. PARP9/DTX3L complex and PARP12 catalyze mono-ADP-ribosylation (MARylation) of viral proteins leading to their proteosomal degradation while PARP10, through binding to avian influenza virus NS1, prevents viral RNA replication. PARP7, -10, -12 and -13 are inhibitors of viral translation stopping the formation of the translation initiation complex on viral mRNA (5)
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