Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration
Target membrane poration is a longstanding enigma in virology. Here, authors show that fusion peptides of the influenza virus’ spike protein aggregate, rotate, and tilt in membranes, facilitating peptide-induced poration during viral fusion.
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-34576-z |
| _version_ | 1811177847915544576 |
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| author | Amy Rice Sourav Haldar Eric Wang Paul S. Blank Sergey A. Akimov Timur R. Galimzyanov Richard W. Pastor Joshua Zimmerberg |
| author_facet | Amy Rice Sourav Haldar Eric Wang Paul S. Blank Sergey A. Akimov Timur R. Galimzyanov Richard W. Pastor Joshua Zimmerberg |
| author_sort | Amy Rice |
| collection | DOAJ |
| description | Target membrane poration is a longstanding enigma in virology. Here, authors show that fusion peptides of the influenza virus’ spike protein aggregate, rotate, and tilt in membranes, facilitating peptide-induced poration during viral fusion. |
| first_indexed | 2024-04-11T06:09:16Z |
| format | Article |
| id | doaj.art-032e71bde5444d9ea7d8158275f55efe |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-11T06:09:16Z |
| publishDate | 2022-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-032e71bde5444d9ea7d8158275f55efe2022-12-22T04:41:22ZengNature PortfolioNature Communications2041-17232022-12-0113111510.1038/s41467-022-34576-zPlanar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting porationAmy Rice0Sourav Haldar1Eric Wang2Paul S. Blank3Sergey A. Akimov4Timur R. Galimzyanov5Richard W. Pastor6Joshua Zimmerberg7Laboratory of Computational Biology, National Heart Lung and Blood Institute, National Institutes of HealthSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of HealthLaboratory of Computational Biology, National Heart Lung and Blood Institute, National Institutes of HealthSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of HealthA.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of SciencesA.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of SciencesLaboratory of Computational Biology, National Heart Lung and Blood Institute, National Institutes of HealthSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of HealthTarget membrane poration is a longstanding enigma in virology. Here, authors show that fusion peptides of the influenza virus’ spike protein aggregate, rotate, and tilt in membranes, facilitating peptide-induced poration during viral fusion.https://doi.org/10.1038/s41467-022-34576-z |
| spellingShingle | Amy Rice Sourav Haldar Eric Wang Paul S. Blank Sergey A. Akimov Timur R. Galimzyanov Richard W. Pastor Joshua Zimmerberg Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration Nature Communications |
| title | Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration |
| title_full | Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration |
| title_fullStr | Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration |
| title_full_unstemmed | Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration |
| title_short | Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration |
| title_sort | planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration promoting poration |
| url | https://doi.org/10.1038/s41467-022-34576-z |
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