Disruption of host antiviral resistances by gammaherpesvirus tegument proteins with homology to the FGARAT purine biosynthesis enzyme.

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.

• Authors: Kevin Tsai, Troy E Messick, Paul M Lieberman
• Journal: Current opinion in virology (Curr Opin Virol) Vol. 14 Pg. 30-40 (Oct 2015) ISSN: 1879-6265 [Electronic] Netherlands
• PMID: 26256000 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)
• Copyright: Copyright © 2015 Elsevier B.V. All rights reserved.

Chemical References

• Viral Structural Proteins
• Phosphoribosylglycinamide Formyltransferase

Topics

• Gammaherpesvirinae (immunology, physiology)
• Host-Pathogen Interactions
• Humans
• Immune Evasion
• Immunity, Innate
• Phosphoribosylglycinamide Formyltransferase (genetics)
• Viral Structural Proteins (genetics, metabolism)