Abstract
The zinc finger antiviral protein (ZAP) restricts the replication of a broad range of RNA and DNA viruses. ZAP directly binds viral RNA, targeting it for degradation and inhibiting its translation. While the full scope of RNA determinants involved in mediating selective ZAP activity is unclear, ZAP binds CpG dinucleotides, dictating at least part of its target specificity. ZAP interacts with many cellular proteins, although only a few have been demonstrated to be essential for its antiviral activity, including the 3'-5' exoribonuclease exosome complex, TRIM25, and KHNYN. In addition to inhibiting viral gene expression, ZAP also directly and indirectly targets a subset of cellular messenger RNAs to regulate the innate immune response. Overall, ZAP protects a cell from viral infection by restricting viral replication and regulating cellular gene expression. Further understanding of the ZAP antiviral system may allow for novel viral vaccine and anticancer therapy development.
Highlights
Vertebrate cells contain several pattern recognition receptors (PRRs) that discriminate between viral and cellular RNA to elicit an antiviral response while avoiding chronic autoimmune activation
As single-stranded RNA (ssRNA) is the predominant form of cellular RNA, zinc finger antiviral protein (ZAP) must be selective in its activity or risk altering global cellular gene expression
Because ZAP-L and ZAP-S have the highest expression levels and their antiviral function is best characterized, this review focuses on these isoforms [5, 6]
Summary
Targeted Restriction of Viral Gene Expression and Replication by the ZAP Antiviral System. ZAP, zinc finger antiviral protein, ZC3HAV1, PARP13, CpG dinucleotide, virus, interferon-stimulated gene
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