On the stability of parainfluenza virus 5 F proteins

J Virol. 2015 Mar;89(6):3438-41. doi: 10.1128/JVI.03221-14. Epub 2015 Jan 14.

Abstract

The crystal structure of the F protein (prefusion form) of the paramyxovirus parainfluenza virus 5 (PIV5) WR isolate was determined. We investigated the basis by which point mutations affect fusion in PIV5 isolates W3A and WR, which differ by two residues in the F ectodomain. The P22 stabilizing site acts through a local conformational change and a hydrophobic pocket interaction, whereas the S443 destabilizing site appears sensitive to both conformational effects and amino acid charge/polarity changes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Crystallography, X-Ray
  • Humans
  • Mutation
  • Parainfluenza Virus 5 / chemistry
  • Parainfluenza Virus 5 / genetics
  • Parainfluenza Virus 5 / metabolism*
  • Protein Stability
  • Protein Structure, Tertiary
  • Rubulavirus Infections / virology
  • Viral Fusion Proteins / chemistry*
  • Viral Fusion Proteins / genetics
  • Viral Fusion Proteins / metabolism

Substances

  • Viral Fusion Proteins

Associated data

  • PDB/2B9B
  • PDB/4GIP