Key result
The zinc finger antiviral protein (ZAP) restricts viral replication by binding viral RNA and targeting it for degradation, and regulates cellular gene expression to modulate the innate immune response.
Why the study?
The full scope of RNA determinants involved in mediating selective ZAP antiviral activity remains unclear.
Understanding the ZAP antiviral system's mechanisms of restricting viral replication and regulating cellular gene expression may inform novel viral vaccine and anticancer therapies.
ZAP-CpG binding may inform future antiviral strategies; leaves open full RNA determinants and essential cofactors.
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.
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Ficarelli et al. (2021) conducted a review in Viral infection. Zinc finger antiviral protein (ZAP) was evaluated. The zinc finger antiviral protein (ZAP) restricts viral replication by binding viral RNA and targeting it for degradation, and regulates cellular gene expression to modulate the innate immune response.
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