On the stability of parainfluenza virus 5 F proteins

Taylor A. Poor, Albert S. Song, Brett D. Welch, Christopher A. Kors, Theodore S. Jardetzky, Robert A. Lamb*

*Corresponding author for this work

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

The crystal structure of the F protein (prefusion form) of the paramyxovirus parainfluenza virus 5 (PIV5)WRisolate was determined. Weinvestigated 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.

Original languageEnglish (US)
Pages (from-to)3438-3441
Number of pages4
JournalJournal of virology
Volume89
Issue number6
DOIs
StatePublished - Jan 1 2015

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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    Poor, T. A., Song, A. S., Welch, B. D., Kors, C. A., Jardetzky, T. S., & Lamb, R. A. (2015). On the stability of parainfluenza virus 5 F proteins. Journal of virology, 89(6), 3438-3441. https://doi.org/10.1128/JVI.03221-14