title: Conformational plasticity of the Ebola virus matrix protein.
abstract: Filoviruses are the causative agents of a severe and often fatal hemorrhagic fever with repeated outbreaks in Africa. They are negative sense single stranded enveloped viruses that can cross species barriers from its natural host bats to primates including humans. The small size of the genome poses limits to viral adaption, which may be partially overcome by conformational plasticity. Here we review the different conformational states of the Ebola virus (EBOV) matrix protein VP40 that range from monomers, to dimers, hexamers, and RNA-bound octamers. This conformational plasticity that is required for the viral life cycle poses a unique opportunity for development of VP40 specific drugs. Furthermore, we compare the structure to homologous matrix protein structures from Paramyxoviruses and Bornaviruses and we predict that they do not only share the fold but also the conformational flexibility of EBOV VP40.
authors.affiliation: University Grenoble Alpes, UVHCI, F-38000, Grenoble, France; CNRS, UVHCI, F-38000, Grenoble, France.
authors.forename: Jens
authors.initials: J
authors.lastname: Radzimanowski
authors.forename: Gregory
authors.initials: G
authors.lastname: Effantin
authors.forename: Winfried
authors.initials: W
authors.lastname: Weissenhorn
mesh_terms: D029043:Ebolavirus / Q000378:metabolism / Q000502:physiology; D008958:Models, Molecular; D009698:Nucleoproteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D011487:Protein Conformation; D014758:Viral Core Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D019065:Virus Assembly; D057074:Virus Release
chemical_list: D009698:Nucleoproteins; D014758:Viral Core Proteins; C084819:nucleoprotein VP40, Ebola virus
keywords: Ebola virus; VP40; assembly; budding