Structure of the zinc-finger antiviral protein in complex with RNA reveals a mechanism for selective targeting of CG-rich viral sequences | Zendy

Jennifer L. Meagher | Zendy; Matthew A. Takata | Zendy; Daniel Gonçalves-Carneiro | Zendy; Sarah C. Keane | Zendy; Antoine Rebendenne | Zendy; Heley Ong | Zendy; Victoria K. Orr | Zendy; Margaret R. MacDonald | Zendy; Jeanne A. Stuckey | Zendy; Paul D. Bieniasz | Zendy; Janet L. Smith | Zendy

Open Access

Structure of the zinc-finger antiviral protein in complex with RNA reveals a mechanism for selective targeting of CG-rich viral sequences

Author(s) -

Jennifer L. Meagher,

Matthew A. Takata,

Daniel Gonçalves-Carneiro,

Sarah C. Keane,

Antoine Rebendenne,

Heley Ong,

Victoria K. Orr,

Margaret R. MacDonald,

Jeanne A. Stuckey,

Paul D. Bieniasz,

Janet L. Smith

Publication year - 2019

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.1913232116

Subject(s) - rna , zinc finger , rna binding protein , biology , riboswitch , nucleic acid structure , microbiology and biotechnology , biochemistry , binding site , chemistry , non coding rna , gene , transcription factor

Significance Zinc finger antiviral protein (ZAP) protects cells from infection by diverse RNA viruses through its ability to specifically detect and deplete viral RNAs that have a greater frequency of CG dinucleotides than host messenger RNAs. We solved an X-ray crystal structure of the domain of ZAP that recognizes RNA and found that a crucial component of RNA recognition by ZAP is a pocket on the protein surface that can accommodate a CG dinucleotide but no other dinucleotides. The structure explains in atomic detail how ZAP is able to selectively recognize CG-rich viral RNAs as foreign and thereby provide hosts with a defense against viral infection.

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