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Nat Commun. 2018 Apr 30;9(1):1736. doi: 10.1038/s41467-018-04058-2.

Promotion of virus assembly and organization by the measles virus matrix protein.

Author information

1
Division of Infectious Diseases, Department of Pediatrics, Emory University School of Medicine, Children's Healthcare of Atlanta, Atlanta, GA, 30322, USA.
2
School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
3
Department of Infectious Diseases, Department of Population Health and Center for Vaccines and Immunology, University of Georgia, Athens, GA, 30602, USA.
4
Institute for Biomedical Sciences, Georgia State University, Atlanta, GA, 30303, USA.
5
Institute for Biomedical Sciences, Georgia State University, Atlanta, GA, 30303, USA. rplemper@gsu.edu.
6
Division of Infectious Diseases, Department of Pediatrics, Emory University School of Medicine, Children's Healthcare of Atlanta, Atlanta, GA, 30322, USA. erwrigh@emory.edu.
7
Robert P. Apkarian Integrated Electron Microscopy Core, Emory University, Atlanta, GA, 30322, USA. erwrigh@emory.edu.

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.

PMID:
29712906
PMCID:
PMC5928126
DOI:
10.1038/s41467-018-04058-2
[Indexed for MEDLINE]
Free PMC Article

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