Host-Mediated Viral Mutations: APOBECs, ADARs, and Beyond

Dear Colleagues,

The apolipoprotein B mRNA-editing enzyme, catalytic polypeptide (APOBEC) family of enzymes is responsible for the deamination of cytosine in single-stranded RNA and DNA. In humans, this family includes 11 members, including APOBEC1, 2, 3A, 3B, 3C, 3D, 3F, 3G, 3H, 4, and activation-induced cytidine deaminase (AID). The functions of these enzymes range from epigenetic modifications of DNA, including removal of methylcytosine and 5-hydroxymethylcytosine, to mutagenesis of host and viral mRNAs. Current evidence suggests that both RNA and DNA viruses are mutagenized by APOBECs, leading to selection and altered pathogenicity. Although APOBECs are typically associated with the innate immune response to viral infections, AID is a primordial member of the family that controls affinity maturation of antibodies as well as effector functions by class switch recombination. Viral manipulation of APOBECs often is observed by enzyme relocalization or degradation, and APOBEC antagonists include both virally specified RNAs and proteins. Adenosine deaminases acting on RNA (ADARs) result in inosine substitutions (A-to-I editing) on double-stranded RNAs. Both APOBECs and ADARs are inducible by interferons and can function in both the cytosol and nucleus to affect both viral and cellular gene function. In addition, multiple viruses, including SARS CoV-2, have been shown to induce the host DNA damage response (DDR), resulting in genomic loss of integrity and inflammation. This issue will address new insights into APOBECs, ADARs, and host DDR for their impact on viral selection and the immune response.

Prof. Dr. Jaquelin P. Dudley
Guest Editor

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