ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations

Biochim Biophys Acta. 2011 Feb;1808(2):572-9. doi: 10.1016/j.bbamem.2010.08.004. Epub 2010 Aug 12.

Abstract

ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9±0.8pS at elevated temperature (38.5°C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Computer Simulation
  • Ion Channels / chemistry*
  • Ion Channels / genetics
  • Lipid Bilayers
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • SARS Virus / chemistry*
  • SARS Virus / genetics
  • Viral Matrix Proteins / chemistry*
  • Viral Matrix Proteins / genetics

Substances

  • Ion Channels
  • Lipid Bilayers
  • Viral Matrix Proteins
  • sars7a protein, SARS virus