N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes.
Biochem Biophys Res Commun
; 477(1): 27-32, 2016 08 12.
Article
em En
| MEDLINE
| ID: mdl-27282484
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.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Vírus da Influenza A
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Proteínas Virais
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Biopolímeros
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Cardiolipinas
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Membrana Celular
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Colesterol
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Amiloide
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
França