Key result
In vitro chemical mapping and isoenergetic microarray techniques demonstrate that the consensus sequence for the 81-148 nucleotide region of the Influenza A NS1 intron folds into a hairpin conformation.
The conserved 81-148 nucleotide region of the influenza A NS1 intron folds into a hairpin structure in vitro, providing a foundation for designing experiments to probe its functional role.
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Does not alter influenza care; leaves open the hairpin's in vivo role and therapeutic potential.
Influenza A virus is a segmented single-stranded (-)RNA virus that causes substantial annual morbidity and mortality. The transcriptome of influenza A is predicted to have extensive RNA secondary structure. The smallest genome segment, segment 8, encodes two proteins, NS1 and NEP, via alternative splicing. A conserved RNA domain in the intron of segment 8 may be important for regulating production of NS1. Two different multi-branch loop structures have been proposed for this region. A combination of in vitro chemical mapping and isoenergetic microarray techniques demonstrate that the consensus sequence for this region folds into a hairpin conformation. These results provide an alternative folding for this region and a foundation for designing experiments to probe its functional role in the influenza life cycle.
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Priore et al. (2013) studied Influenza A. In vitro chemical mapping and isoenergetic microarrays was evaluated on RNA secondary structure of the 81-148 nucleotide region. In vitro chemical mapping and isoenergetic microarray techniques demonstrate that the consensus sequence for the 81-148 nucleotide region of the Influenza A NS1 intron folds into a hairpin conformation.
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