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Conformational flexibility in the enterovirus RNA replication platform.

Meghan S Warden1, Kai Cai2, Gabriel Cornilescu3

  • 1Department of Chemistry and Biochemistry, Old Dominion University, Norfolk, Virginia 23529, USA.

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The enterovirus 5

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • The 5' cloverleaf (5'CL) RNA structure initiates enterovirus genomic replication.
  • Stem-loop B (SLB) and stem-loop D (SLD) within the 5'CL are crucial for protein interactions.
  • Understanding 5'CL structure is key to viral replication mechanisms.

Purpose of the Study:

  • To determine the solution structure of the rhinovirus serotype 14 5'CL.
  • To investigate the conformational changes of the 5'CL in response to magnesium ions.
  • To elucidate how structural changes facilitate protein interactions essential for viral replication.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy.
  • Small-angle X-ray scattering (SAXS).

Main Results:

  • The 5'CL adopts an open conformation without magnesium.
  • Magnesium binding induces compaction, bringing SLB and SLD into close proximity.
  • This compaction creates an accessible major groove surface for protein binding.

Conclusions:

  • Magnesium-dependent structural rearrangements of the 5'CL are critical for viral replication.
  • The compact structure facilitates essential protein-RNA interactions.
  • This study provides structural insights into enterovirus replication initiation.