Abstract:
:All known gammaherpesviruses encode at least one conserved tegument protein that contains sequence homology to the cellular purine biosynthesis enzyme: phosphoribosylformylglycineamide amidotransferase (FGARAT, or PFAS). While no enzymatic activity have been found on these viral FGARAT-homology proteins (vFGARAT), they are important for disarming host intrinsic antiviral machinery. Most vFGARAT proteins disrupt the intrinsic antiviral response-associated cellular subnuclear structure: ProMyelocytic Leukemia (PML) associated nuclear body (PML-NB). vFGARATs from different viruses target different components of PML-NB to prevent cellular repression of viral infection. In addition, vFGARATs of rhadinoviruses were recently found to oligomerize with the cellular FGARAT to deamidate RIG-I and repress inflammatory cytokine production. In this review we discuss the diverse mechanisms of antiviral response disruption by gammaherpesvirus vFGARATs and the significance of the enzyme homology domain.
journal_name
Curr Opin Viroljournal_title
Current opinion in virologyauthors
Tsai K,Messick TE,Lieberman PMdoi
10.1016/j.coviro.2015.07.008subject
Has Abstractpub_date
2015-10-01 00:00:00pages
30-40eissn
1879-6257issn
1879-6265pii
S1879-6257(15)00106-6journal_volume
14pub_type
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