This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Loney, C.
Right arrow Articles by Bhella, D.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Loney, C.
Right arrow Articles by Bhella, D.

 Previous Article  |  Next Article 

Journal of Virology, August 2009, p. 8191-8197, Vol. 83, No. 16
0022-538X/09/$08.00+0     doi:10.1128/JVI.00693-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Paramyxovirus Ultrastructure and Genome Packaging: Cryo-Electron Tomography of Sendai Virus {triangledown} ,{dagger}

Colin Loney,1 Geneviève Mottet-Osman,2 Laurent Roux,2 and David Bhella1*

Medical Research Council Virology Unit, University of Glasgow, Church Street, Glasgow G11 5JR, United Kingdom,1 Department of Microbiology and Molecular Medicine, University of Geneva, Faculty of Medicine, CMU, 1 rue Michel-Servet, 1211 Geneva 4, Switzerland2

Received 3 April 2009/ Accepted 3 June 2009

Members of the Paramyxoviridae such as measles, mumps, and parainfluenza viruses have pleomorphic, enveloped virions that contain negative-sense unsegmented RNA genomes. This is encapsidated by multiple copies of a viral nucleocapsid protein N to form a helical ribonucleoprotein complex (termed the nucleocapsid), which acts as the template for both transcription and replication. Structure analysis of these viruses has proven challenging, owing to disordered regions in important constituent proteins, conformational flexibility in the nucleocapsid and the pleomorphic nature of virus particles. We conducted a low-resolution ultrastructural analysis of Sendai virus, a prototype paramyxovirus, using cryo-electron tomography. Virions are highly variable in size, ranging approximately from 110 to 540 nm in diameter. Envelope glycoproteins are densely packed on the virion surface, while nucleocapsids are clearly resolved in the virion interior. Subtomogram segmentation and filament tracing allowed us to define the path of many nucleocapsids and in some cases to determine the number of putative genomes within a single virus particle. Our findings indicate that these viruses may contain between one and six copies of their genome per virion and that there is no discernible order to nucleocapsid packaging.


* Corresponding author. Mailing address: Medical Research Council Virology Unit, University of Glasgow, Church Street, Glasgow G11 5JR, United Kingdom. Phone: 44-141-330-3685. Fax: 44-141-337-2236. E-mail: d.bhella{at}mrcvu.gla.ac.uk

{triangledown} Published ahead of print on 3 June 2009.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.


Journal of Virology, August 2009, p. 8191-8197, Vol. 83, No. 16
0022-538X/09/$08.00+0     doi:10.1128/JVI.00693-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.