Species-Specific Deamidation of cGAS by Herpes Simplex Virus UL37 Protein Facilitates Viral Replication.

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 Microbe

journal_title

Cell host & microbe

authors

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 P

doi

10.1016/j.chom.2018.07.004

subject

Has Abstract

pub_date

2018-08-08 00:00:00

pages

234-248.e5

issue

2

eissn

1931-3128

issn

1934-6069

pii

S1931-3128(18)30374-3

journal_volume

24

pub_type

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