Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81154
Title: N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes
Authors: Ajjaji, Dalila
Richard, Charles-Adrien
Mazerat, Sandra
Chevalier, Christophe
Vidic, Jasmina
Keywords: PB1-F2-Membrane interaction
Influenza A viruses
Amyloid-like protein structures
Cholesterol
Cardiolipin
Issue Date: 2016
Source: Ajjaji, D., Richard, C.-A., Mazerat, S., Chevalier, C., & Vidic, J. (2016). N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes. Biochemical and Biophysical Research Communications, 477(1), 27-32.
Series/Report no.: Biochemical and Biophysical Research Communications
Abstract: PB1-F2 protein is a factor of virulence of influenza A viruses which increases the mortality and morbidity associated with infection. Most seasonal H1N1 Influenza A viruses express nowadays a truncated version of PB1-F2. Here we show that truncation of PB1-F2 modified supramolecular organization of the protein in a membrane-mimicking environment. In addition, full-length PB1-F2(1–90) and C-terminal PB1-F2 domain (53–90), efficiently permeabilized various anionic liposomes while N-terminal domain PB1-F2(1–52) only lysed cholesterol and cardiolipin containing lipid bilayers. These findings suggest that the truncation of PB1-F2 may impact the pathogenicity of a given virus strain.
URI: https://hdl.handle.net/10356/81154
http://hdl.handle.net/10220/40672
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2016.06.016
Rights: © 2016 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Biochemical and Biophysical Research Communications, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/j.bbrc.2016.06.016].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:MSE Journal Articles

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