Journal
JOURNAL OF VIROLOGY
Volume 90, Issue 4, Pages 1839-1848Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01597-15
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Funding
- Japan Society for Promotion of Science
- Health and Labor Sciences Research Grants, Japan
- HHS \ National Institutes of Health (NIH) [AI081077]
- HHS \ NIH \ National Institute of Allergy and Infectious Diseases (NIAID) [R44 AI08843]
- Ministry of Education, Culture, Sports, Science, and Technology (MEXT)
- HHS \ NIH \ National Institute of General Medical Sciences (NIGMS) [T32GM075762]
- Burroughs Wellcome Fund (BWF)
- NIH/NIAID [R44 AI08843]
- Investigators in the Pathogenesis of Infectious Disease award from the Burroughs Wellcome Fund
- NIH [AI081077, T32GM075762]
- Japan Society for the Promotion of Science
- Ministry of Education, Culture, Sports, Science, and Technology
- PRESTO from Japan Science and Technology Agency
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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.
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