Journal Article

Macrodomain ADP-ribosylhydrolase and the pathogenesis of infectious diseases

Leung, Anthony K. L., McPherson, Robert Lyle, Griffin, Diane E.

2018

Overview

[...]ectopic expression of the alphaviral macrodomain-containing nsP3 protein inhibits the formation of stress granules-a class of cytoplasmic structures with antiviral functions (e.g., [37]; reviewed in [38]). [...]most virus-induced PARPs add MARylation, while all viral macrodomains remove MARylation. [...]one intriguing hypothesis is that while viral macrodomains can bind ADP-ribosylation added by host PARPs, viruses may circumvent host defenses or regulate replication by removing specific classes of ADP-ribosylation (Fig 3). [...]besides the macrodomain family, there is another major class of ADP-ribosylation removal enzyme called DraG/ARH, and they are also found in all kingdoms of life, including viruses [42,50]. Unlike MacroD-type macrodomains, which remove ADP-ribosylation from acidic residues, ARH members remove ADP-ribosylation from arginine [51] and serine [43,52]. [...]one can speculate that pathogens may have multiple enzymes to remove ADP-ribosylation from specific classes of amino acids.

• Publisher: Public Library of Science,Public Library of Science (PLoS)
• Subject: Adenosine diphosphate / Amino acids / Animals / Biochemistry / Biology and life sciences / Chikungunya virus / Communicable diseases / Ectopic expression / Host-Pathogen Interactions / Humans / Infectious diseases / Medicine and Health Sciences / Molecular biology / Mutation / N-Glycosyl Hydrolases - physiology / Pathogenesis / Pathogenic microorganisms / Pearls / Physical sciences / Proteins / Proteomics / Public health / Virulence / Virus Diseases - enzymology / Virus Diseases - virology / Virus Replication / Viruses / Viruses - pathogenicity