N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes
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...
| Main Authors: | , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
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2016
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| Online Access: | https://hdl.handle.net/10356/81154 http://hdl.handle.net/10220/40672 |
| _version_ | 1826128456648228864 |
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| author | Ajjaji, Dalila Richard, Charles-Adrien Mazerat, Sandra Chevalier, Christophe Vidic, Jasmina |
| author2 | School of Materials Science & Engineering |
| author_facet | School of Materials Science & Engineering Ajjaji, Dalila Richard, Charles-Adrien Mazerat, Sandra Chevalier, Christophe Vidic, Jasmina |
| author_sort | Ajjaji, Dalila |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T07:25:16Z |
| format | Journal Article |
| id | ntu-10356/81154 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:25:16Z |
| publishDate | 2016 |
| record_format | dspace |
| spelling | ntu-10356/811542023-07-14T15:49:43Z N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes Ajjaji, Dalila Richard, Charles-Adrien Mazerat, Sandra Chevalier, Christophe Vidic, Jasmina School of Materials Science & Engineering 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. Accepted version 2016-06-14T03:28:07Z 2019-12-06T14:22:34Z 2016-06-14T03:28:07Z 2019-12-06T14:22:34Z 2016 2016 Journal Article Ajjaji, D., Richard, C.-A., Mazerat, S., Chevalier, C., & Vidic, J. (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. Biochemical and Biophysical Research Communications, 477(1), 27-32. 0006-291X https://hdl.handle.net/10356/81154 http://hdl.handle.net/10220/40672 10.1016/j.bbrc.2016.06.016 194706 en Biochemical and Biophysical Research Communications © 2016 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Biochemical and Biophysical Research Communications, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/j.bbrc.2016.06.016]. 21 p. application/pdf |
| spellingShingle | PB1-F2-Membrane interaction Influenza A viruses Amyloid-like protein structures Cholesterol Cardiolipin Ajjaji, Dalila Richard, Charles-Adrien Mazerat, Sandra Chevalier, Christophe Vidic, Jasmina N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes |
| title | N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes |
| title_full | N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes |
| title_fullStr | N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes |
| title_full_unstemmed | N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes |
| title_short | N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes |
| title_sort | n terminal domain of pb1 f2 protein of influenza a virus can fold into amyloid like oligomers and damage cholesterol and cardiolipid containing membranes |
| topic | PB1-F2-Membrane interaction Influenza A viruses Amyloid-like protein structures Cholesterol Cardiolipin |
| url | https://hdl.handle.net/10356/81154 http://hdl.handle.net/10220/40672 |
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