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

• Type of Material: Article
• Authors: Zunlong Ke, Emory University; Joshua D. Strauss, Emory University; Cheri M. Hampton, Emory University; Melinda A. Brindley, University of Georgia; Rebecca S. Dillard, Emory University; Fredrick Leon, Emory University; Kristen M. Lamb, Emory University; Richard Karl Plemper, Emory University; Elizabeth R. Wright, Emory University
• Language: English
• Date: 2018-04-30
• Publisher: Nature Publishing Group: Nature Communications
• Publication Version: Final Published Version
• Copyright Statement: © 2018 The Author(s).
• License: Creative Commons Attribution 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1038/s41467-018-04058-2
• Title of Journal or Parent Work: Nature Communications
• ISSN: 2041-1723
• Volume: 9
• Start Page: 1736
• End Page: 1736
• Grant/Funding Information: This work was supported in part by Emory University; Children’s Healthcare of Atlanta; the Georgia Research Alliance; the Center for AIDS Research at Emory University (P30 AI050409); the James B. Pendleton Charitable Trust to E.R.W.; public health service grants R01AI083402 and R01HD079327 to R.K.P., R01GM114561 and R21AI101775 to E. R. W., F32GM112517 to J.D.S., and NSF grant 0923395 to E.R.W.
• Keywords: Multidisciplinary Sciences; CRYOTOMOGRAPHY; ELECTRON-MICROSCOPY; F-PROTEIN; Science & Technology - Other Topics; Science & Technology; VISUALIZATION; CRYOELECTRON TOMOGRAPHY; INTACT VIRIONS; NUCLEOCAPSIDS; MEMBRANE-FUSION; CELL-FUSION; GLYCOPROTEIN
• Research Categories: Health Sciences, Immunology; Biology, Virology; Biology, Microbiology

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.