Ebola and Marburg virus matrix layers are locally ordered assemblies of VP40 dimers.
William Wan, Mairi Clarke, Michael J Norris, Larissa Kolesnikova, Alexander Koehler, Zachary A Bornholdt, Stephan Becker, Erica Ollmann Saphire, John Ag Briggs
Author Information
William Wan: Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany. ORCID
Mairi Clarke: Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany. ORCID
Michael J Norris: Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, La Jolla, United States. ORCID
Larissa Kolesnikova: Institut für Virologie, Philipps-Universität Marburg, Hans-Meerwein-Straße, Marburg, Germany.
Alexander Koehler: Institut für Virologie, Philipps-Universität Marburg, Hans-Meerwein-Straße, Marburg, Germany.
Zachary A Bornholdt: The Scripps Research Institute, La Jolla, United States. ORCID
Stephan Becker: Institut für Virologie, Philipps-Universität Marburg, Hans-Meerwein-Straße, Marburg, Germany.
Erica Ollmann Saphire: Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, La Jolla, United States. ORCID
John Ag Briggs: Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany. ORCID
Filoviruses such as Ebola and Marburg virus bud from the host membrane as enveloped virions. This process is achieved by the matrix protein VP40. When expressed alone, VP40 induces budding of filamentous virus-like particles, suggesting that localization to the plasma membrane, oligomerization into a matrix layer, and generation of membrane curvature are intrinsic properties of VP40. There has been no direct information on the structure of VP40 matrix layers within viruses or virus-like particles. We present structures of Ebola and Marburg VP40 matrix layers in intact virus-like particles, and within intact Marburg viruses. VP40 dimers assemble extended chains via C-terminal domain interactions. These chains stack to form 2D matrix lattices below the membrane surface. These lattices form a patchwork assembly across the membrane and suggesting that assembly may begin at multiple points. Our observations define the structure and arrangement of the matrix protein layer that mediates formation of filovirus particles.
