Key result
Nuclear magnetic resonance spectroscopy revealed that human rhinovirus isotype 14 SLB adopts a predominantly A-form helical structure with a highly disordered pyrimidine-rich loop region.
The solution structure of human rhinovirus isotype 14 SLB reveals a predominantly A-form helical structure with a disordered pyrimidine-rich loop region, providing insights into viral replication mechanisms.
May guide picornavirus replication inhibitor design; leaves open cellular validation studies.
The presumptive RNA cloverleaf at the start of the 5'-untranslated region of the picornavirus genome is an essential element in replication. Stem loop B (SLB) of the cloverleaf is a recognition site for the host polyC-binding protein, which initiates a switch from translation to replication. Here we present the solution structure of human rhinovirus isotype 14 SLB using nuclear magnetic resonance spectroscopy. SLB adopts a predominantly A-form helical structure. The stem contains five Watson-Crick base pairs and one wobble base pair and is capped by an eight-nucleotide loop. The wobble base pair introduces perturbations into the helical parameters but does not appear to introduce flexibility. However, the helix major groove appears to be accessible. Flexibility is seen throughout the loop and in the terminal nucleotides. The pyrimidine-rich region of the loop, the apparent recognition site for the polyC-binding protein, is the most disordered region of the structure.
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Warden et al. (2017) studied Picornavirus replication. Nuclear magnetic resonance spectroscopy revealed that human rhinovirus isotype 14 SLB adopts a predominantly A-form helical structure with a highly disordered pyrimidine-rich loop region.
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