Structure and Functions of the Ebola Virus Matrix Protein VP40

Abstract

The matrix protein VP40 of the highly pathogenic Ebola virus (EBOV), a member of the filovirus family, is the most abundant protein in EBOV virions. During the viral life cycle it mediates assembly and budding from the host cell, and is responsible for the characteristic filamentous shape of EBOV particles. In addition to this classical function as a matrix protein, VP40 was also shown to have a regulatory function in viral transcription. To enable these distinct functions, VP40 can adopt different oligomeric states, in particular, dimers, hexamers and ring-like octameric RNA-binding structures. This review describes the properties and functions of the EBOV matrix protein VP40 and how these different conformations of VP40 contribute to its diverse functions.

Keywords: :

• budding
• Ebola virus
• filovirus
• matrix protein
• oligomers
• structure
• VP40

Author contributions

Original draft was written by L Wendt, J Brandt and T Hoenen. L Wendt, J Brandt and T Hoenen were responsible for review and editing. Visualization was done by L Wendt, J Brandt and T Hoenen. Funding acquisition was done by T Hoenen.

Financial & competing interests disclosure

Funding was provided by the Friedrich-Loeffler-Institut, German Federal Research Institute for Animal Health and by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) – grant number 389002253. The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.

No writing assistance was utilized in the production of this manuscript.