N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes

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...

Full description

Saved in:
Bibliographic Details
Main Authors: Ajjaji, Dalila, Richard, Charles-Adrien, Mazerat, Sandra, Chevalier, Christophe, Vidic, Jasmina
Other Authors: School of Materials Science & Engineering
Format: Article
Language:English
Published: 2016
Subjects:
Online Access:https://hdl.handle.net/10356/81154
http://hdl.handle.net/10220/40672
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-81154
record_format dspace
spelling sg-ntu-dr.10356-811542023-07-14T15:49:43Z N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes Ajjaji, Dalila Richard, Charles-Adrien Mazerat, Sandra Chevalier, Christophe Vidic, Jasmina School of Materials Science & Engineering PB1-F2-Membrane interaction Influenza A viruses Amyloid-like protein structures Cholesterol Cardiolipin 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. Accepted version 2016-06-14T03:28:07Z 2019-12-06T14:22:34Z 2016-06-14T03:28:07Z 2019-12-06T14:22:34Z 2016 2016 Journal Article 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. 0006-291X https://hdl.handle.net/10356/81154 http://hdl.handle.net/10220/40672 10.1016/j.bbrc.2016.06.016 194706 en Biochemical and Biophysical Research Communications © 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]. 21 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic PB1-F2-Membrane interaction
Influenza A viruses
Amyloid-like protein structures
Cholesterol
Cardiolipin
spellingShingle PB1-F2-Membrane interaction
Influenza A viruses
Amyloid-like protein structures
Cholesterol
Cardiolipin
Ajjaji, Dalila
Richard, Charles-Adrien
Mazerat, Sandra
Chevalier, Christophe
Vidic, Jasmina
N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes
description 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.
author2 School of Materials Science & Engineering
author_facet School of Materials Science & Engineering
Ajjaji, Dalila
Richard, Charles-Adrien
Mazerat, Sandra
Chevalier, Christophe
Vidic, Jasmina
format Article
author Ajjaji, Dalila
Richard, Charles-Adrien
Mazerat, Sandra
Chevalier, Christophe
Vidic, Jasmina
author_sort Ajjaji, Dalila
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
title_short N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes
title_full N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes
title_fullStr N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes
title_full_unstemmed N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes
title_sort n-terminal domain of pb1-f2 protein of influenza a virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes
publishDate 2016
url https://hdl.handle.net/10356/81154
http://hdl.handle.net/10220/40672
_version_ 1772828249192136704