On the stability of parainfluenza virus 5 F proteins.

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.

• Authors: Taylor A Poor, Albert S Song, Brett D Welch, Christopher A Kors, Theodore S Jardetzky, Robert A Lamb
• Journal: Journal of virology (J Virol) Vol. 89 Issue 6 Pg. 3438-41 (Mar 2015) ISSN: 1098-5514 [Electronic] United States
• PMID: 25589638 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2015, American Society for Microbiology. All Rights Reserved.

Chemical References

• Viral Fusion Proteins

Topics

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