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

Zunlong Ke, Joshua D. Strauss, Cheri M. Hampton, Melinda A. Brindley, Rebecca S. Dillard, Fredrick Leon, Kristen M. Lamb, Richard K. Plemper () and Elizabeth R. Wright ()
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Zunlong Ke: Children’s Healthcare of Atlanta
Joshua D. Strauss: Children’s Healthcare of Atlanta
Cheri M. Hampton: Children’s Healthcare of Atlanta
Melinda A. Brindley: University of Georgia
Rebecca S. Dillard: Children’s Healthcare of Atlanta
Fredrick Leon: Children’s Healthcare of Atlanta
Kristen M. Lamb: Children’s Healthcare of Atlanta
Richard K. Plemper: Georgia State University
Elizabeth R. Wright: Children’s Healthcare of Atlanta

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-04058-2

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