Interacting motif networks located in hotspots associated with RNA release are conserved in Enterovirus capsids

FEBS Lett. 2017 Jun;591(12):1687-1701. doi: 10.1002/1873-3468.12663. Epub 2017 May 22.

Abstract

Enteroviruses are responsible for a multitude of human diseases. Expansion of the virus capsid is associated with a cascade of conformational changes that allow the subsequent release of RNA. For the first time, this study presents a comprehensive bioinformatic screen for the prediction of interacting motifs within intraprotomer interfaces and across respective interfaces surrounding the fivefold and twofold axes. The results identify a network of conserved motif residues involved in interactions in enteroviruses that may be critical to capsid stabilisation, providing guidelines towards developing antivirals that interfere with viral expansion during RNA release.

Keywords: Enterovirus; RNA release; alanine scan; conserved motifs; structural proteins.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Capsid Proteins / chemistry
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism*
  • Computational Biology
  • Conserved Sequence
  • Crystallography, X-Ray
  • Databases, Protein
  • Energy Transfer
  • Enterovirus / metabolism*
  • Models, Molecular*
  • Mutation
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Stability
  • Protein Subunits / chemistry
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • RNA, Viral / chemistry
  • RNA, Viral / metabolism*
  • Rhinovirus / metabolism*
  • Species Specificity
  • Surface Properties

Substances

  • Capsid Proteins
  • Protein Subunits
  • RNA, Viral