tetano
Editor, Senior Moderator
Biochem Biophys Res Commun. 2016 Jun 6. pii: S0006-291X(16)30934-2. doi: 10.1016/j.bbrc.2016.06.016. [Epub ahead of print]
[h=1]N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes.[/h] Ajjaji D[SUP]1[/SUP], Richard CA[SUP]2[/SUP], Mazerat S[SUP]3[/SUP], Chevalier C[SUP]4[/SUP], Vidic J[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
Copyright ? 2016. Published by Elsevier Inc.
[h=4]KEYWORDS:[/h] Amyloid-like protein structures; Cardiolipin; Cholesterol; Influenza A viruses; PB1-F2-Membrane interaction
PMID: 27282484 [PubMed - as supplied by publisher]
[h=1]N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes.[/h] Ajjaji D[SUP]1[/SUP], Richard CA[SUP]2[/SUP], Mazerat S[SUP]3[/SUP], Chevalier C[SUP]4[/SUP], Vidic J[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
Copyright ? 2016. Published by Elsevier Inc.
[h=4]KEYWORDS:[/h] Amyloid-like protein structures; Cardiolipin; Cholesterol; Influenza A viruses; PB1-F2-Membrane interaction
PMID: 27282484 [PubMed - as supplied by publisher]