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.
Type de document :
Article dans une revue
Protein Science, Wiley, 2014, pp.1519-27
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Contributeur : Frank Thomas <>
Soumis le : mercredi 10 décembre 2014 - 15:34:13
Dernière modification le : lundi 11 février 2019 - 16:51:20


  • HAL Id : hal-01093367, version 1
  • PUBMED : 25159197



Jens Radzimanowski, Grégory Effantin, Winfried Weissenhorn. Conformational plasticity of the Ebola virus matrix protein.. Protein Science, Wiley, 2014, pp.1519-27. 〈hal-01093367〉



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