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MMI Faculty

Michele Barry, PhD

Michele Barry, PhD
Dept. of Medical Microbiology & Immunology
University of Alberta
Faculty of Medicine & Dentistry
6-21 Heritage Medical Research Centre
T6G 2S2 Edmonton, AB

Ph : (780) 492-0702
Fx : (780) 492-9828


**Dr. Barry is not accepting students at this time**


  • Professor, Dept. of Medical Microbiology & Immunology
  • Canada Research Chair Tier I
  • Howard Hughes International Scholar
  • Executive Committee Member - Li Ka Shing Institute of Virology
  • Journal of Virology - Associate Editor (2011-2013)
  • PLOS Pathogen Editorial Board - Associate Editor
  • AHFMR Senior Scholar
  • CIHR - New Investigator
  • Member, Faculty Research Committee, Faculty of Medicine and Dentistry
  • Immunology Network Council Member


Hide and Seek: Unraveling the Strategies Viruses Use to Evade Detection

During the course of evolution, viruses have adapted to ensure their own survival by exploiting and manipulating cellular signaling pathways, thereby preventing the host from detecting and destroying them. The study of viral immune evasion can identify previously unknown aspects of the host immune response. To understand more about virus:host interactions we study poxviruses. Poxviruses are a family of double-stranded DNA-containing viruses that replicate within the cytoplasm of the cell and encode over 200 proteins. The most notorious member of the family is variola virus, which prior to eradiation was the causative agent of smallpox. This family of viruses has proven to be extremely adept at counteracting host immune responses and interfering with host cell signaling pathways. Our main focus is to understanding how poxviruses manipulate cellular signaling pathways and specifically how poxviruses regulate cell death and exploit the ubiquitin proteasome pathway.

Poxvirus Inhibition of Cell Death- Research in my laboratory is currently focused on understanding how members of the poxviruses family evade apoptosis. Apoptosis is an inherent cellular property that can be triggered by a variety of external stimuli including cytotoxic T lymphocytes and in some instances virus infection itself. The impairment of apoptotic pathways is a key event controlled by many pathogens. Therefore, in order to ensure their own survival, viruses have evolved strategies that target crucial components within the apoptotic cascade and have proven to be important tools for dissecting apoptotic pathways. Several years ago we identified a novel anti-apoptotic protein, F1L, encoded by vaccinia virus (PNAS 100:14345 ). Despite lacking apparent sequence similarity to members of the cellular Bcl-2 family, F1L localizes to the mitochondria and inhibits the release of cytochrome c. F1L functions by inhibiting both Bak and Bax, the key pro-apoptotic proteins that are essential for initiating cell death (J. Biol. Chem. 281:39728). In contrast to F1L, the avipoxviruses, which include fowlpox virus, are the only poxviruses known to encode proteins with obvious Bcl-2 sequence homology (J. Virology 81:11032). We have found that fowlpox virus inhibits apoptosis by inactivating multiple pro-apoptotic Bcl-2 proteins including some BH3-only proteins as well as Bax and Bak (J. Virology 83:7085).


Cytochrome c Release During Apoptosis

Cytochrome c Release During Apoptosis



Vaccinia Virus F1L localizes to mitochondria


Poxvirus Exploitation of the Ubiquitin Proteasome Pathway- Ubiquitin is a 76 amino acid protein that plays a crucial role in protein degradation. The covalent attachment of ubiquitin to target substrates results in protein degradation or dramatic alterations in protein function. The process of ubiquitination is essential for cellular homeostasis, and tightly regulates a wide range of cellular functions, such as the cell cycle, signal transduction, transcription, and DNA repair. A large family of cellular ubiquitin ligases is responsible for transferring ubiquitin to specific substrates. Recently we have found that poxviruses exploit the ubiquitination machinery by expressing viral proteins that function as ubiquitin ligases or regulate cellular ubiquitin ligases. These include p28, a poxvirus encoded RING-containing protein that functions as an ubiquitin ligase (J. Virology 79:597), viral encoded proteins that interact with cellular cullin-3 ubiquitin to regulate ubiquitination of currently unknown substrates (Virology 374:82). More recently, my lab has identified a unique family of F-box proteins in poxviruses that interact with the cellular SCF ubiquitin ligase complex (J. Virology 82:9917). Since our research has shown that poxviruses encode a number of proteins that regulate the ubiquitin proteasome pathway, we investigated the role of the 26S proteasome during poxvirus infection. Inhibition of the proteasome resulted in a dramatic defect in poxvirus replication indicating that the proteasome and ubiquitin are required for poxvirus infection (J. Virology 83:2099).




Cullin-1 and cullin-3 ubiquitin ligases.

Barry and Fruh, Science STKE 335:pe21



  • Ninad Mehta (Graduate Student)



Click here for most recent publications


Selected Publications:

  1. Rintoul, J.L., J. Wang, D. B. Gammon, N. van Buuren, K. Garson, M. Barry, D. H. Evans, and J. C. Bell. 2011. Site-specific Recombination Using a Controlled Marker Stabilization System for the Engineering of Marker-free Recombinant Poxviruses. PLOS One, 6(9):e24643.

  2. Marcet-Palacios. M., B. L.Duggan, I. Shostak, M. Barry, T. Geskes, J. A. Wilkins, A. Yanagiya, N. Sonenberg, and R. C. Bleackley. 2011. Granzyme B Inhibits Translation Vaccinia Virus Production Through Proteolytic Cleavage of Eukaryotic Initiation Factor 4 Gamma 3. PLOS pathogen, 7(12):e1002447.

  3. Banadyga L, Lam SC, Okamoto T, Kvansakul M, Huang DC, Barry M. Deerpox Virus Encodes an Inhibitor of Apoptosis that Regulates Bak and Bax. J Virol. 2011 Jan;85(2):883-94. Epub 2010 Oct 27

  4. Fagan-Garcia K, Barry M. A vaccinia virus deletion mutant reveals the presence of additional inhibitors of NF-kappaB. J Virol. 2010 Dec 15 [Epub ahead of print]

  5. Barry M, N. VanBuuren, K Burles, K Mottet, Q Wang, and A Teale. 2010. Poxvirus Exploitation of the Ubiquitin-Proteasome System. Viruses 2:2356-2380

  6. Banadyga L and M Barry. 2010. A Matter of Life and Death: Viruses Inhibit Cell Suicide. Biology on the Cutting Edge. Concepts Issues and Canadian Research Around the Globe. Editors S.L. Gilles and S. Hewitt. Pearson Canada Inc, Toronto, Ontario, Canada, pg. 153-157.

  7. Campbell, S, Hazes B, Kvansakul, M, Colman P, Barry, M. Vaccinia virus F1L interacts with Bak using highly divergent BCL-2 homology domains and replaces the function of Mcl-1. 2010 J Biol. Chem. 258:4695-708

  8. Banadyga, L, Veugelers K, Campbell S, Barry M. The fowlpox virus BCL-2 homologue, FPV039, interacts with activated Bax and a discrete subset of BH3-only proteins to inhibit apoptosis. 2009. J Virol. 83:7085-98.

  9. Teale A, Campbell S, Van Buuren N, Magee WC, Watmough K, Couturier B, Shipclark R, Barry M. Orthopoxviruses require a functional ubiquitin-proteasome system for productive replication. 2009. J Virol. 83:2099-108

  10. Mohamed MR, Rahman MM, Lanchbury JS, Shattuck D, Neff C, Dufford M, Van Buuren N, Fagan K, Barry M, Smith S, Damon I, McFadden G. Proteomic screening of variola virus reveals a unique NF-kappaB inhibitor that is highly conserved among pathogenic orthopoxviruses. Proc Natl Acad Sci U S A. 2009. 106:9045-50.

  11. Van Buuren, N., Couturier, B., Xiong, Y. and Barry, M. Ectromelia virus encodes a novel family of F-box proteins that interact with the SCF complex. 2008. J. Virol. 82:9917-9927.

  12. Wilton, B. A., Campbell, S., Van Buuren, N., Garneau, R., Furukawa, M., Xiong, Y. and Barry, M. Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases. 2008. Virology 374:82-99

  13. Banadyga L, Gerig J, Stewart T, Barry M.  Fowlpox virus encodes a Bcl-2 homologue that protects cells from apoptotic death through interaction with the proapoptotic protein Bak. 2007. J Virol. 81:11032-45.

  14. Taylor JM, Quilty D, Banadyga L, Barry M.  The vaccinia virus protein F1L interacts with Bim and inhibits activation of the proapoptotic protein Bax. 2006. 
    J Biol Chem. 281:39728-39.

  15. Barry M., Fruh K. Viral modulators of cullin RING ubiquitin ligases: culling the host defense. 2006.  Science STKE.(335):pe21.

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