{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Amiar S"],"funding":["National Institute of Allergy and Infectious Diseases","NIAID NIH HHS","National Institutes of Health Office of the Director","National Institutes of Health","National Institute of General Medical Sciences","NIH HHS","Division of Intramural Research"],"pagination":["100663"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11565396"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["65(11)"],"pubmed_abstract":["Plasma membrane (PM) domains and order phases have been shown to play a key role in the assembly, release, and entry of several lipid-enveloped viruses. In the present study, we provide a mechanistic understanding of the Ebola virus (EBOV) matrix protein VP40 interaction with PM lipids and their effect on VP40 oligomerization, a crucial step for viral assembly and budding. VP40 matrix formation is sufficient to induce changes in the PM fluidity. We demonstrate that the distance between the lipid headgroups, the fatty acid tail saturation, and the PM order are important factors for the stability of VP40 binding and oligomerization at the PM. The use of FDA-approved drugs to fluidize the PM destabilizes the viral matrix assembly leading to a reduction in budding efficiency. Overall, these fi"],"journal":["Journal of lipid research"],"pubmed_title":["A fatty acid-ordered plasma membrane environment is critical for Ebola virus matrix protein assembly and budding."],"pmcid":["PMC11565396"],"funding_grant_id":["R01 AI081077","S10OD027034","S10 OD027043","R01AI081077","T32GM075762"],"pubmed_authors":["Stahelin RV","Johnson KA","Husby ML","Amiar S","Marzi A"],"additional_accession":[]},"is_claimable":false,"name":"A fatty acid-ordered plasma membrane environment is critical for Ebola virus matrix protein assembly and budding.","description":"Plasma membrane (PM) domains and order phases have been shown to play a key role in the assembly, release, and entry of several lipid-enveloped viruses. In the present study, we provide a mechanistic understanding of the Ebola virus (EBOV) matrix protein VP40 interaction with PM lipids and their effect on VP40 oligomerization, a crucial step for viral assembly and budding. VP40 matrix formation is sufficient to induce changes in the PM fluidity. We demonstrate that the distance between the lipid headgroups, the fatty acid tail saturation, and the PM order are important factors for the stability of VP40 binding and oligomerization at the PM. The use of FDA-approved drugs to fluidize the PM destabilizes the viral matrix assembly leading to a reduction in budding efficiency. Overall, these fi","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-07-16T22:37:43.611Z","creation":"2025-04-06T01:42:01.046Z"},"accession":"S-EPMC11565396","cross_references":{"pubmed":["39369791"],"doi":["10.1016/j.jlr.2024.100663"]}}