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.
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CITATION STYLE
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
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