Crystal structure of an adenovirus virus-associated RNA

Iris V. Hood, Jackson M. Gordon, Charles Bou-Nader, Frances E. Henderson, Soheila Bahmanjah and Jinwei Zhang ()
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Iris V. Hood: National Institute of Diabetes and Digestive and Kidney Diseases
Jackson M. Gordon: National Institute of Diabetes and Digestive and Kidney Diseases
Charles Bou-Nader: National Institute of Diabetes and Digestive and Kidney Diseases
Frances E. Henderson: National Institute of Diabetes and Digestive and Kidney Diseases
Soheila Bahmanjah: National Institute of Diabetes and Digestive and Kidney Diseases
Jinwei Zhang: National Institute of Diabetes and Digestive and Kidney Diseases

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Adenovirus Virus-Associated (VA) RNAs are the first discovered viral noncoding RNAs. By mimicking double-stranded RNAs (dsRNAs), the exceptionally abundant, multifunctional VA RNAs sabotage host machineries that sense, transport, process, or edit dsRNAs. How VA-I suppresses PKR activation despite its strong dsRNA character, and inhibits the crucial antiviral kinase to promote viral translation, remains largely unknown. Here, we report a 2.7 Å crystal structure of VA-I RNA. The acutely bent VA-I features an unusually structured apical loop, a wobble-enriched, coaxially stacked apical and tetra-stems necessary and sufficient for PKR inhibition, and a central domain pseudoknot that resembles codon-anticodon interactions and prevents PKR activation by VA-I. These global and local structural features collectively define VA-I as an archetypal PKR inhibitor made of RNA. The study provides molecular insights into how viruses circumnavigate cellular rules of self vs non-self RNAs to not only escape, but further compromise host innate immunity.

Date: 2019
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DOI: 10.1038/s41467-019-10752-6

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