The native structure of the full-length, assembled influenza A virus matrix protein, M1
Influenza A virus causes millions of severe illnesses during annual epidemics. The most abundant protein in influenza virions is the matrix protein M1 that mediates virus assembly by forming an endoskeleton beneath the virus membrane. The structure of full-length M1, and how it oligomerizes to mediate assembly of virions, is unknown. Here we have determined the complete structure of assembled M1 within intact virus particles, as well as the structure of M1 oligomers reconstituted in vitro. We found that the C-terminal domain of M1 is disordered in solution, but can fold and bind in trans to the N-terminal domain of another M1 monomer, thus polymerising M1 into linear strands which coat the interior surface of the assembling virion membrane. In the M1 polymer, five histidine residues, contributed by three different M1 monomers, form a cluster that can serve as the pH-sensitive disassembly switch after entry into a target cell. These structures therefore provide mechanisms for influenza virus assembly and disassembly..
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Preprint| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
bioRxiv.org - (2021) vom: 15. Dez. Zur Gesamtaufnahme - year:2021 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Peukes, Julia [VerfasserIn] |
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| doi: |
10.1101/2020.06.24.168567 |
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| PPN (Katalog-ID): |
XBI018213960 |
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| 245 | 1 | 0 | |a The native structure of the full-length, assembled influenza A virus matrix protein, M1 |
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| 520 | |a Influenza A virus causes millions of severe illnesses during annual epidemics. The most abundant protein in influenza virions is the matrix protein M1 that mediates virus assembly by forming an endoskeleton beneath the virus membrane. The structure of full-length M1, and how it oligomerizes to mediate assembly of virions, is unknown. Here we have determined the complete structure of assembled M1 within intact virus particles, as well as the structure of M1 oligomers reconstituted in vitro. We found that the C-terminal domain of M1 is disordered in solution, but can fold and bind in trans to the N-terminal domain of another M1 monomer, thus polymerising M1 into linear strands which coat the interior surface of the assembling virion membrane. In the M1 polymer, five histidine residues, contributed by three different M1 monomers, form a cluster that can serve as the pH-sensitive disassembly switch after entry into a target cell. These structures therefore provide mechanisms for influenza virus assembly and disassembly. | ||
| 700 | 1 | |a Xiong, Xiaoli |e verfasserin |4 aut | |
| 700 | 1 | |a Erlendsson, Simon |e verfasserin |4 aut | |
| 700 | 1 | |a Qu, Kun |e verfasserin |4 aut | |
| 700 | 1 | |a Wan, William |e verfasserin |4 aut | |
| 700 | 1 | |a Calder, Leslie J. |e verfasserin |4 aut | |
| 700 | 1 | |a Schraidt, Oliver |e verfasserin |4 aut | |
| 700 | 1 | |a Kummer, Susann |e verfasserin |4 aut | |
| 700 | 1 | |a Freund, Stefan M. V. |e verfasserin |4 aut | |
| 700 | 1 | |a Kräusslich, Hans-Georg |e verfasserin |4 aut | |
| 700 | 1 | |a Briggs, John A. G. |e verfasserin |4 aut | |
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