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

• 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: PB1-F2-Membrane interaction; Influenza A viruses; Amyloid-like protein structures; Cholesterol; Cardiolipin
• Online Access: https://hdl.handle.net/10356/81154; http://hdl.handle.net/10220/40672
• Institution: Nanyang Technological University

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.