This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Spehner, D.
Right arrow Articles by Rziha, H.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Spehner, D.
Right arrow Articles by Rziha, H.-J.

 Previous Article  |  Next Article 

Journal of Virology, August 2004, p. 8085-8093, Vol. 78, No. 15
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.15.8085-8093.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Appearance of the Bona Fide Spiral Tubule of Orf Virus Is Dependent on an Intact 10-Kilodalton Viral Protein

D. Spehner,1* S. De Carlo,2 R. Drillien,1 F. Weiland,3 K. Mildner,3 D. Hanau,1 and H.-J. Rziha3*

INSERM E 0345, EFS-Alsace, 67065 Strasbourg, France,1 Centre de Microscopie Electronique de l'Université de Lausanne, 1005 Lausanne, Switzerland,2 Bundesforschungsanstalt für Viruskrankheiten der Tiere, Institut für Immunologie, 72076 Tübingen, Germany3

Received 19 December 2003/ Accepted 30 March 2004

Parapoxviruses can be morphologically distinguished from other poxviruses in conventional negative staining electron microscopy (EM) by their ovoid appearance and the spiral tubule surrounding the virion's surface. However, this technique may introduce artifacts. We have examined Orf virus (ORFV; the prototype species of the Parapoxvirus genus) by cryoelectron microscopy (cryo-EM) and cryo-negative staining EM. From these studies we suggest that the shape and unique spiral tubule are authentic features of the parapoxviruses. We also constructed an ORFV mutant deleted of a gene encoding a 10-kDa protein, which is an orthologue of the vaccinia virus (VACV) 14-kDa fusion protein, and investigated its ultrastructure. This mutant virus multiplied slowly in permissive cells and produced infectious but morphologically aberrant particles. Mutant virions lacked the spiral tubule but displayed short disorganized tubules similar to those observed on the surface of VACV. In addition, thin extensions or loop-like structures were appended to the ORFV mutant particles. We suggest that these appended structures arise from a failure of the mutant virus particles to properly seal and that the sealing activity is dependent on the 10-kDa protein.


* Corresponding author. Mailing address for Hanns-Joachim Rziha: Bundesforschungsanstalt für Viruskrankheiten der Tiere, Institut für Immunologie, Paul-Ehrlich Strasse 28, 72076 Tübingen, Germany. Phone: 49 7071 967 253. Fax: 49 7071 967 303. E-mail: achim.rziha{at}tue.bfav.de. Mailing address for Danièle Spehner: INSERM EPI 99-08, EFS-Alsace, 10 rue Spielmann, 67065 Strasbourg, France. Phone: 33 3 88 21 25 25. Fax: 33 3 88 21 25 44. E-mail: daniele.spehner{at}efs-alsace.fr.


Journal of Virology, August 2004, p. 8085-8093, Vol. 78, No. 15
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.15.8085-8093.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Tan, J. L., Ueda, N., Mercer, A. A., Fleming, S. B. (2009). Investigation of orf virus structure and morphogenesis using recombinants expressing FLAG-tagged envelope structural proteins: evidence for wrapped virus particles and egress from infected cells. J. Gen. Virol. 90: 614-625 [Abstract] [Full Text]  
  • Kuznetsov, Y., Gershon, P. D., McPherson, A. (2008). Atomic Force Microscopy Investigation of Vaccinia Virus Structure. J. Virol. 82: 7551-7566 [Abstract] [Full Text]  
  • Hyun, J.-K., Coulibaly, F., Turner, A. P., Baker, E. N., Mercer, A. A., Mitra, A. K. (2007). The Structure of a Putative Scaffolding Protein of Immature Poxvirus Particles as Determined by Electron Microscopy Suggests Similarity with Capsid Proteins of Large Icosahedral DNA Viruses. J. Virol. 81: 11075-11083 [Abstract] [Full Text]  
  • Heuser, J. (2005). Deep-etch EM reveals that the early poxvirus envelope is a single membrane bilayer stabilized by a geodetic "honeycomb" surface coat. JCB 169: 269-283 [Abstract] [Full Text]