N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes - INRA - Institut national de la recherche agronomique
Article Dans Une Revue Biochemical and Biophysical Research Communications Année : 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

Résumé

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.
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N-terminal%20domain%20of%20PB1-F2%20protein%20of%20influenza%20A%20virus%20can%20fold%20into%20amyloid-like%20oligomers%20and%20damage%20cholesterol%20and%20cardiolipid%20containing%20membranes.pdf (527.16 Ko) Télécharger le fichier
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Dates et versions

hal-02636639 , version 1 (18-09-2024)

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Dalila Ajjaji, Charles-Adrien Richard, Sandra Mazerat, Christophe Chevalier, Jasmina Vidic. 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, 2016, 477 (1), pp.27-32. ⟨10.1016/j.bbrc.2016.06.016⟩. ⟨hal-02636639⟩
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