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Protein Sci. 2014 Nov;23(11):1519-27. doi: 10.1002/pro.2541. Epub 2014 Sep 4.

Conformational plasticity of the Ebola virus matrix protein.

Author information

1
University Grenoble Alpes, UVHCI, F-38000, Grenoble, France; CNRS, UVHCI, F-38000, Grenoble, France.

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.

KEYWORDS:

Ebola virus; VP40; assembly; budding

PMID:
25159197
PMCID:
PMC4241103
DOI:
10.1002/pro.2541
[Indexed for MEDLINE]
Free PMC Article

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