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

doi:10.1128/JVI.03221-14

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

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	3438-3441
Number of pages	4
Journal	Journal of virology
Volume	89
Issue number	6
DOIs	https://doi.org/10.1128/JVI.03221-14
State	Published - 2015

ASJC Scopus subject areas

Microbiology
Immunology
Insect Science
Virology

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title = "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)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.",

author = "Poor, {Taylor A.} and Song, {Albert S.} and Welch, {Brett D.} and Kors, {Christopher A.} and Jardetzky, {Theodore S.} and Lamb, {Robert A.}",

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T1 - On the stability of parainfluenza virus 5 F proteins

AU - Poor, Taylor A.

AU - Song, Albert S.

AU - Welch, Brett D.

AU - Kors, Christopher A.

AU - Jardetzky, Theodore S.

AU - Lamb, Robert A.

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

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AN - SCOPUS:84923167132

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SP - 3438

EP - 3441

JO - Journal of Virology

JF - Journal of Virology

IS - 6

ER -

On the stability of parainfluenza virus 5 F proteins

Abstract

ASJC Scopus subject areas

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