Abstract
Virus infection has been consistently threatening public health. The cyclic GMP-AMP synthase (cGAS)-Stimulator of Interferon Genes (STING) pathway is a critical defender to sense various pathogens and trigger innate immunity of mammalian cells. cGAS recognizes the pathogenic DNA in the cytosol and then synthesizes 2′3′-cyclic GMP-AMP (2′3′cGAMP). As the second messenger, cGAMP activates STING and induces the following cascade to produce type I interferon (IFN-I) to protect against infections. However, viruses have evolved numerous strategies to hinder the cGAS-STING signal transduction, promoting their immune evasion. Here we outline the current status of the viral evasion mechanism underlying the regulation of the cGAS-STING pathway, focusing on how post-transcriptional modifications, viral proteins, and non-coding RNAs involve innate immunity during viral infection, attempting to inspire new targets discovery and uncover potential clinical antiviral treatments.
Highlights
Infectious diseases are the top threats to public health
The present review provides potential worth evaluating targets in innate immune response that are viable in clinical trials and antiviral reagents development for current and future studies
Compared with other coronaviral proteins, papain-like protease (PLpro) contributes to both virus replication and host cell signaling-cascade regulation, which is more suitable to be a target for antiviral drug design (Baez-Santos et al, 2015)
Summary
Infectious diseases are the top threats to public health. With the persistent invading of various pathogens, mammalians have developed certain strategies to protect themselves from extraneous risks. Several studies showed that viruses benefit from hijacking host enzymes to alter the modification of antiviral immune cGAS-STING in Viral Evasion cascades component proteins, conducive to their replication (Carty et al, 2021; Hong et al, 2021; Song et al, 2021). Infected by DNA virus, the Myb-like, SWIRM, and MPN domains 1 protein (MYSM1) is increasingly expressed and interacts with STING, leading to the removal of K63linked ubiquitination STING at Lys150 to down-regulate STING signaling (Tian et al, 2020).
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