Cryo-electron tomography of Marburg Virus particles and their morphogenesis within infected cells

Bharat, Tanmay A. M., Riches, James D., Kolesnikova, Larissa, Welsch, Sonja, Krähling, Verena, Davey, Norman, Rey, Félix A., Parsy, Marie-Laure, Becker, Stephan, & Briggs, John A. G. (2011) Cryo-electron tomography of Marburg Virus particles and their morphogenesis within infected cells. PL o S Biology (Online), 9(11), e1001196-e1001196.

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Abstract

Several major human pathogens, including the filoviruses, paramyxoviruses, and rhabdoviruses, package their single-stranded RNA genomes within helical nucleocapsids, which bud through the plasma membrane of the infected cell to release enveloped virions. The virions are often heterogeneous in shape, which makes it difficult to study their structure and assembly mechanisms. We have applied cryo-electron tomography and sub-tomogram averaging methods to derive structures of Marburg virus, a highly pathogenic filovirus, both after release and during assembly within infected cells. The data demonstrate the potential of cryo-electron tomography methods to derive detailed structural information for intermediate steps in biological pathways within intact cells. We describe the location and arrangement of the viral proteins within the virion. We show that the N-terminal domain of the nucleoprotein contains the minimal assembly determinants for a helical nucleocapsid with variable number of proteins per turn. Lobes protruding from alternate interfaces between each nucleoprotein are formed by the C-terminal domain of the nucleoprotein, together with viral proteins VP24 and VP35. Each nucleoprotein packages six RNA bases. The nucleocapsid interacts in an unusual, flexible "Velcro-like" manner with the viral matrix protein VP40. Determination of the structures of assembly intermediates showed that the nucleocapsid has a defined orientation during transport and budding. Together the data show striking architectural homology between the nucleocapsid helix of rhabdoviruses and filoviruses, but unexpected, fundamental differences in the mechanisms by which the nucleocapsids are then assembled together with matrix proteins and initiate membrane envelopment to release infectious virions, suggesting that the viruses have evolved different solutions to these conserved assembly steps.

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ID Code: 57663
Item Type: Journal Article
Refereed: Yes
Additional URLs:
Keywords: cryo electron tomography, marburg virus, ebola virus
DOI: 10.1371/journal.pbio.1001196
ISSN: 1545-7885 (online)
Subjects: Australian and New Zealand Standard Research Classification > BIOLOGICAL SCIENCES (060000) > BIOCHEMISTRY AND CELL BIOLOGY (060100) > Structural Biology (incl. Macromolecular Modelling) (060112)
Australian and New Zealand Standard Research Classification > BIOLOGICAL SCIENCES (060000) > MICROBIOLOGY (060500) > Virology (060506)
Divisions: Current > Institutes > Institute for Future Environments
Copyright Owner: Copyright 2011 The authors.
Copyright Statement: This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Deposited On: 26 Feb 2013 23:41
Last Modified: 13 Jul 2013 05:21

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