Abstract:
:Herpes simplex virus 1 (HSV-1) establishes infections in humans and mice, but some non-human primates exhibit resistance via unknown mechanisms. Innate immune recognition pathways are highly conserved but are pivotal in determining susceptibility to DNA virus infections. We report that variation of a single amino acid residue in the innate immune sensor cGAS determines species-specific inactivation by HSV-1. The HSV-1 UL37 tegument protein deamidates human and mouse cGAS. Deamidation impairs the ability of cGAS to catalyze cGAMP synthesis, which activates innate immunity. HSV-1 with deamidase-deficient UL37 promotes robust antiviral responses and is attenuated in mice in a cGAS- and STING-dependent manner. Mutational analyses identified a single asparagine in human and mouse cGAS that is not conserved in many non-human primates. This residue underpins UL37-mediated cGAS deamidation and species permissiveness of HSV-1. Thus, HSV-1 mediates cGAS deamidation for immune evasion and exploits species sequence variation to disarm host defenses.
journal_name
Cell Host Microbejournal_title
Cell host & microbeauthors
Zhang J,Zhao J,Xu S,Li J,He S,Zeng Y,Xie L,Xie N,Liu T,Lee K,Seo GJ,Chen L,Stabell AC,Xia Z,Sawyer SL,Jung J,Huang C,Feng Pdoi
10.1016/j.chom.2018.07.004subject
Has Abstractpub_date
2018-08-08 00:00:00pages
234-248.e5issue
2eissn
1931-3128issn
1934-6069pii
S1931-3128(18)30374-3journal_volume
24pub_type
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