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

作者：Ajjaji Dalila; Richard Charles Adrien; Mazerat Sandra; Chevalier Christophe^*; Vidic Jasmina^*

来源：Biochemical and Biophysical Research Communications, 2016, 477(1): 27-32.

DOI：10.1016/j.bbrc.2016.06.016

• 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.

• 出版日期2016-8-12
• 单位南阳理工学院