5B0V

Crystal Structure of Marburg virus VP40 Dimer

Summary for 5B0V

• Entry DOI: 10.2210/pdb5b0v/pdb
• Descriptor: Matrix protein VP40, ETHANOL (3 entities in total)
• Functional Keywords: marburg virus, virus assembly protein, immunosuppression, filovirus, viral protein
• Biological source: Lake Victoria marburgvirus (strain Musoke-80) (MARV)
• Cellular location: Virion membrane ; Peripheral membrane protein: P35260
• Total number of polymer chains: 2
• Total formula weight: 72080.79

Authors

Oda, S.,Bornholdt, Z.A.,Abelson, D.M.,Saphire, E.O. (deposition date: 2015-11-05, release date: 2016-01-20, Last modification date: 2024-11-13)

Primary citation

Oda, S.,Noda, T.,Wijesinghe, K.J.,Halfmann, P.,Bornholdt, Z.A.,Abelson, D.M.,Armbrust, T.,Stahelin, R.V.,Kawaoka, Y.,Saphire, E.O.
Crystal Structure of Marburg Virus VP40 Reveals a Broad, Basic Patch for Matrix Assembly and a Requirement of the N-Terminal Domain for Immunosuppression
J.Virol., 90:1839-1848, 2015

PubMed Abstract: Marburg virus (MARV), a member of the filovirus family, causes severe hemorrhagic fever with up to 90% lethality. MARV matrix protein VP40 is essential for assembly and release of newly copied viruses and also suppresses immune signaling in the infected cell. Here we report the crystal structure of MARV VP40. We found that MARV VP40 forms a dimer in solution, mediated by N-terminal domains, and that formation of this dimer is essential for budding of virus-like particles. We also found the N-terminal domain to be necessary and sufficient for immune antagonism. The C-terminal domains of MARV VP40 are dispensable for immunosuppression but are required for virus assembly. The C-terminal domains are only 16% identical to those of Ebola virus, differ in structure from those of Ebola virus, and form a distinct broad and flat cationic surface that likely interacts with the cell membrane during virus assembly.

PubMed: 26656687
DOI: 10.1128/JVI.01597-15

Experimental method

X-RAY DIFFRACTION (2.81 Å)