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 Barrett, J. W.
Right arrow Articles by McFadden, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Barrett, J. W.
Right arrow Articles by McFadden, G.

 Previous Article  |  Next Article 

Journal of Virology, January 2007, p. 106-114, Vol. 81, No. 1
0022-538X/07/$08.00+0     doi:10.1128/JVI.01633-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

M135R Is a Novel Cell Surface Virulence Factor of Myxoma Virus{triangledown}

John W. Barrett, Joanna Sypula, Fuan Wang, Lindsay R. Alston, Zhuhong Shao, Xiujuan Gao, Timothy S. Irvine, and Grant McFadden*

Biotherapeutics Research Group, Robarts Research Institute and Department of Microbiology and Immunology, University of Western Ontario, 1400 Western Road, London, Ontario N6G 2V4, Canada

Received 31 July 2006/ Accepted 11 October 2006

Myxoma virus (MV) encodes a cell surface protein (M135R) that is predicted to mimic the host alpha/beta interferon receptor (IFN-{alpha}/ß-R) and thus prevent IFN-{alpha}/ß from triggering a host antiviral response. This prediction is based on sequence similarity to B18R, the viral IFN-{alpha}/ß-R from vaccinia virus (VV), which has been demonstrated to bind and inhibit type I interferons. However, M135R is only half the size of VV B18R. All other poxvirus-encoded IFN-{alpha}/ß-R homologs align only to the amino-terminal half of M135R. Peptide antibodies raised against M135R were used for immunoblotting and immunofluorescence and indicate that M135R is expressed as an early gene and that the product is a cell surface N-linked glycoprotein that is not secreted. In contrast to the predicted properties of M135R as an inhibitor of type I interferon, all binding and inhibition assays designed to demonstrate whether M135R can interact with IFN-{alpha}/ß have been negative. However, pathogenesis studies with a targeted M135-knockout MV construct (vMyx135KO) indicate that the deletion of M135R severely attenuates MV pathogenesis in the European rabbit. We propose that M135R is an important immunomodulatory virulence factor for myxomatosis but that the target immune ligand is not from the predicted type I interferon family and remains to be identified.

* Corresponding author. Mailing address: Biotherapeutics Research Group, Robarts Research Institute and Department of Microbiology and Immunology, University of Western Ontario, 1400 Western Road, Room 126, London, ON N6G 2V4, Canada. Phone: (519) 663-3932. Fax: (519) 663-3715. E-mail: mcfadden{at}robarts.ca.

{triangledown} Published ahead of print on 25 October 2006.

Journal of Virology, January 2007, p. 106-114, Vol. 81, No. 1
0022-538X/07/$08.00+0     doi:10.1128/JVI.01633-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Morales, M., Ramirez, M. A., Cano, M. J., Parraga, M., Castilla, J., Perez-Ordoyo, L. I., Torres, J. M., Barcena, J. (2009). Genome Comparison of a Nonpathogenic Myxoma Virus Field Strain with Its Ancestor, the Virulent Lausanne Strain. J. Virol. 83: 2397-2403 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»