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  • The EMBO Journal (2000) 19, 4228 - 4236
  • doi:10.1093/emboj/19.16.4228

Crystal structure of the matrix protein VP40 from Ebola virus

Andréa Dessen1,2, Viktor Volchkov3, Olga Dolnik3, Hans-Dieter Klenk3 and Winfried Weissenhorn1

  1. European Molecular Biology Laboratory (EMBL) Grenoble Outstation, 6 rue Jules Horowitz, 38000 Grenoble, France
  2. Present address: Institut de Biologie Structurale, 41 rue Jules Horowitz, 38027 Grenoble, France
  3. Institut für Virologie, Klinikum der Philipps-Universität, Robert-Koch-Strasse 17, D-35037 Marburg, Germany

Correspondence to:

Winfried Weissenhorn, E-mail: weissen@embl-grenoble.fr

Received 11 May 2000; Accepted 26 June 2000; Revised 23 June 2000

Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 Å resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers. Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed.

  • Keywords:

    • crystal structure,
    • Ebola virus,
    • matrix protein,
    • membrane association,
    • VP40