Filovirus proteins for antiviral drug discovery: Structure/function of proteins involved in assembly and budding

There are no approved medications for the treatment of Marburg or Ebola virus infection. In two previous articles (Martin et al., 2016, Martin et al., 2017), we reviewed surface glycoprotein and replication proteins structure/function relationship to decipher the molecular mechanisms of filovirus li...

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Bibliographic Details
Published in:Antiviral research 2018-02, Vol.150, p.183-192
Main Authors: Martin, Baptiste, Reynard, Olivier, Volchkov, Viktor, Decroly, Etienne
Format: Article
Language:English
Subjects:
Antiviral therapy
Bacteriology
Ebola virus
Filovirus
Immunology
Life Sciences
Marburg virus
Microbiology and Parasitology
Mononegavirales
Virion assembly
Virology
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Summary:There are no approved medications for the treatment of Marburg or Ebola virus infection. In two previous articles (Martin et al., 2016, Martin et al., 2017), we reviewed surface glycoprotein and replication proteins structure/function relationship to decipher the molecular mechanisms of filovirus life cycle and identify antiviral strategies. In the present article, we recapitulate knowledge about the viral proteins involved in filovirus assembly and budding. First we describe the structural data available for viral proteins associated with virus assembly and virion egress and then, we integrate the structural features of these proteins in the functional context of the viral replication cycle. Finally, we summarize recent advances in the development of innovative antiviral strategies to target filovirus assembly and egress. The development of such prophylactic or post-exposure treatments could help controlling future filovirus outbreaks. •This review is the third of a series recapitulating knowledge on filovirus protein structure/function relationship.•VP24 and NP orchestrate the assembly and oligomerization of filovirus nucleocapsid.•Filoviruses hijack the cellular multi-vesicular bodies pathway in order to ensure the budding of viral particles.•Budding of filoviruses is driven by a bipartite late domain present into VP40 and/or NP, and GP facilitates virus egress.•Assembly and budding represent innovative targets for the development of innovative antiviral therapies.
ISSN:0166-3542
1872-9096
DOI:10.1016/j.antiviral.2017.12.022