Viral ADP-Ribosylhydrolase
ADP-ribosylation of proteins is a covalent modification that can be induced during a cellular antiviral response to inhibit viral replication. Some RNA viruses have macrodomains embedded in their polyproteins that reverse cellular ADP-ribosylation, potentially counteracting their antiviral effects.
Depending on the virus family, a different type of
ADP-ribosylation might exerts its antiviral effect. Togaviridae are attacked by host PARP10
. The situation could be similar for Hepeviridae and Matonaviridae, which share many characteristics with togaviruses. Coronaviridae may be attacked by several host PARPs, including PARP12
.
Enzymatic reaction:
Viral ADP-Ribosylhydrolase activity is performed by Macro domain that can bind ADP-ribose (an NAD metabolite).
-Mono-ADP-Ribosylhydrolase (MAR hydrolase): Rhea: 58256
Domain:
Viral Macro domain IPR044371
Macro domains IPR002589
Mechanism:
Viral Macro Domains Reverse Protein ADP-Ribosylation
Changqing Li, Yannick Debing, Gytis Jankevicius, Johan Neyts, Ivan Ahel, Bruno Coutard, Bruno Canard.
J Virol. 2016 Sep 12;90(19):8478-86.
The SARS-CoV-2 Conserved Macrodomain Is a Mono-ADP-Ribosylhydrolase
Yousef M O Alhammad, Maithri M Kashipathy, Anuradha Roy, Jean-Philippe Gagn?, Peter McDonald, Philip Gao, Louis Nonfoux, Kevin P Battaile, David K Johnson, Erik D Holmstrom, Guy G Poirier, Scott Lovell, Anthony R Fehr.
J Virol. 2021 Jan 13;95(3):e01969-20.
Mono-ADP-ribosylation by PARP10 inhibits Chikungunya virus nsP2 proteolytic activity and viral replication.
Sarah Krieg, Fabian Pott, Laura Potthoff, Maud Verheirstraeten, Mareike B?tepage, Alexandra Golzmann, Barbara Lippok, Christine Goffinet, Bernhard L?scher, Patricia Korn.
Cell Mol Life Sci. 2023 Feb 25;80(3):72.
PARP12 is required to repress the replication of a Mac1 mutant coronavirus in a cell- and tissue-specific manner.
Catherine M Kerr , Srivatsan Parthasarathy, Nancy Schwarting, Joseph J O'Connor, Jessica J Pfannenstiel, Emily Giri, Sunil More, Robin C Orozco, Anthony R Fehr.
J Virol. 2023 Sep 28;97(9):e0088523.