EMD-7587

Subtomogram averaging
45.0 Å
EMD-7587 Deposition: 19/03/2018
Map released: 09/05/2018
Last modified: 25/12/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-7587

Promotion of Virus Assembly and Organization by the Measles Virus Matrix Protein: F Lattice (recMeV)

EMD-7587

Subtomogram averaging
45.0 Å
EMD-7587 Deposition: 19/03/2018
Map released: 09/05/2018
Last modified: 25/12/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Measles virus
Sample: Measles virus

Deposition Authors: Ke Z, Strauss JD, Hampton CM, Dillard RS, Wright ER
Promotion of virus assembly and organization by the measles virus matrix protein.
Ke Z , Strauss JD, Hampton CM, Brindley MA, Dillard RS, Leon F, Lamb KM, Plemper RK, Wright ER
(2018) Nat Commun , 9 , 1736 - 1736
PUBMED: 29712906
DOI: doi:10.1038/s41467-018-04058-2
ISSN: 2041-1723
Abstract:
Measles virus (MeV) remains a major human pathogen, but there are presently no licensed antivirals to treat MeV or other paramyxoviruses. Here, we use cryo-electron tomography (cryo-ET) to elucidate the principles governing paramyxovirus assembly in MeV-infected human cells. The three-dimensional (3D) arrangement of the MeV structural proteins including the surface glycoproteins (F and H), matrix protein (M), and the ribonucleoprotein complex (RNP) are characterized at stages of virus assembly and budding, and in released virus particles. The M protein is observed as an organized two-dimensional (2D) paracrystalline array associated with the membrane. A two-layered F-M lattice is revealed suggesting that interactions between F and M may coordinate processes essential for MeV assembly. The RNP complex remains associated with and in close proximity to the M lattice. In this model, the M lattice facilitates the well-ordered incorporation and concentration of the surface glycoproteins and the RNP at sites of virus assembly.