ArticleNucleic acids research2003
Solution structure of the influenza A virus cRNA promoter: implications for differential recognition of viral promoter structures by RNA-dependent RNA polymerase.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Characterizing hydrogen bonds in intact RNA from MS2 bacteriophage using magic angle spinning NMR.Biophysical reports · 2021Article
- Cytoplasm and Beyond: Dynamic Innate Immune Sensing of Influenza A Virus by RIG-I.Journal of virology · 2019Review
- Structural and Functional Motifs in Influenza Virus RNAs.Frontiers in microbiology · 2018Review
- Influenza virus segment 5 (+)RNA - secondary structure and new targets for antiviral strategies.Scientific reports · 2017Article
- Influenza virus activation of the interferon system.Virus research · 2015Review
- Targeting Influenza A Virus RNA Promoter.Chemical biology & drug design · 2015Article
- The N-terminal region of influenza virus polymerase PB1 adjacent to the PA binding site is involved in replication but not transcription of the viral genome.Frontiers in microbiology · 2013Article
- Structural characterization of the viral and cRNA panhandle motifs from the infectious salmon anemia virus.Journal of virology · 2011Article
- Residues of the rotavirus RNA-dependent RNA polymerase template entry tunnel that mediate RNA recognition and genome replication.Journal of virology · 2011Article
- Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A virus replication requires the interaction of viral RNA-dependent RNA polymerase (RdRp) with promoters in both the RNA genome (vRNA) and the full-length complementary RNA (cRNA) which serve as templates for the generation of new vRNAs. Although RdRp binds both promoters effectively, it must also discriminate between them because they serve different functional roles in the viral life cycle. Even though the inherent asymmetry between two RNA promoters is considered as a cause of the differential recognition by the RdRp, the structural basis for the ability of the RdRp to recognize the RNA promoters and discriminate effectively between them remains unsolved. Here we report the structure of the cRNA promoter of influenza A virus as determined by heteronuclear magnetic resonance spectroscopy. The terminal region is extremely unstable and does not have a rigid structure. The major groove of the internal loop is widened by the displacement of a novel A*(UU) motif toward the minor groove. These internal loop residues show distinguishable dynamic characters, with differing motional timescales for each residue. Comparison of the cRNA promoter structure with that of the vRNA promoter reveals common structural and dynamic elements in the internal loop, but also differences that provide insight into how the viral RdRp differentially recognizes the cRNA and vRNA promoters.
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