Zinc-finger Antiviral protein (ZAP) is an important antiviral factor encoded by the host. ZAP can specifically inhibit many viruses including mouse leukemia virus, HIV virus, Ebola virus, etc. copy. ZAP specifically binds to the target RNA sequence of the virus and interferes with the translation initiation of the target mRNA. The sequence characteristics and molecular mechanism of ZAP recognition RNA have always been urgently to be solved.
Scientists in China conducted crystal screening of truncated bodies of different ZAP proteins and single-stranded RNA complexes of different sequences and different lengths rich in cytosine and guanine (CG) dinucleotides, and finally obtained a resolution of 2.19Ã… The crystal structure of the ZAP protein N-terminal domain (NZAP) and 6-nt (CGUCGU) single-stranded RNA complex.
Based on this structure, the researchers confirmed the importance of ZAP specific sites for RNA binding and antiviral function. The study also found that multiple ZAP-binding motifs on a viral RNA can make it bind to multiple ZAP protein molecules at the same time. It is speculated that multiple ZAP molecules bind to a single RNA and recruit different downstream cytokines respectively to cooperate RNA degradation function.
In summary, this work reveals in depth the characteristics of ZAP recognition RNA sequences and the molecular pattern of interaction, and the high-resolution crystal structure of the ZAP N-terminal antiviral main functional domain and CG dinucleotide-rich single-stranded RNA complex The molecular basis of ZAP's recognition of CG dinucleotides, single guanine nucleotides and single cytosine nucleotides in single-stranded RNA is explained, which is of great significance for understanding ZAP's antiviral mechanism and eukaryotic gene expression regulation mechanism.
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