کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2473244 | 1555912 | 2015 | 11 صفحه PDF | دانلود رایگان |
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: Current Opinion in Virology - Volume 14, October 2015, Pages 30–40