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

By Dalila Ajjaji, Charles-Adrien Richard, Sandra Mazerat, Charles-Adrien Richard, Jasmina Vidi

July 28, 2017

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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

Author

Dalila Ajjaji, Charles-Adrien Richard, Sandra Mazerat, Charles-Adrien Richard, Jasmina Vidi

Year

2016

Journal

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.

Full Article

http://www.sciencedirect.com/science/article/pii/S0006291X16309342

Instrument

J-810

Keywords

Circular dichroism, Secondary structure, Biochemistry