Adjunct & Associate #90
B. Sc. Université Laval (1980)
Ph. D. Université Laval (1985)
Postdoctoral, Friedrich Miescher Inst., Switzerland (1986-90)
Research Scientist, Agriculture and Agri-Food Canada
- Vancouver Research Centre (1990-1996)
- Pacific Agri-Food Research Centre, Summerland (1996-now)
Associate Editor, Botany
Head, Secoviridae Study Group, International Committee for the Taxonomy of Viruses (ICTV)
Elected Member, Executive Committee, ICTV
Link 1. Nepovirus replication cycle, background information
Link 2. Recent research highlights
Link 3. Sanfacon lab alumni
Link 4. Complete list of publications
Molecular plant virology. Functional studies of viral proteinases, assembly of viral replication complexes, interaction of plant viruses with RNA silencing and design of novel antiviral strategies.
My research program is aimed at providing a molecular understanding of the replication cycle of plant viruses, with the long-term objective of designing new antiviral strategies. In particular, we are studying the function of viral proteins and the interaction between viruses and their host plants.
Tomato ringspot virus (ToRSV) is a nepovirus and an important pathogen of fruit trees and small fruits in North America. Our laboratory is dissecting various steps of the replication cycle. In recent years, we have (1) examined the function and cleavage site specificity of the viral proteinase; (2) studied the assembly of viral replication complexes and examined the interaction between viral replication proteins and intracellular membranes, and (3) characterized the interaction between ToRSV and the plant gene silencing pathway. We have also collaborated with Dr. Thierry Wetzel (AlPlanta, Germany) to study the proteinase and replication proteins of Arabis mosaic virus(ArMV, another nepovirus that causes serious diseases in grapevine in Europe and elsewhere). We use a combination of molecular biology, cellular biology, biochemistry and plant tissue culture techniques.
In response to the discovery of Plum pox virus in Canada (PPV, the causal agent of sharka disease, a devastating disease of Prunus species in Europe), we have also participated in a team research effort to develop resistance to PPV in Prunus germlines.
Wetzel, T., Chisholm, J., Bassler, A. and Sanfacon, H. (2008) Characterization of proteinase cleavage sites in the N-terminal region of the RNA1-encoded polyprotein from Arabis mosaic virus (subgroup A nepovirus). Virology 375, 159-169
Jovel J., Walker M. and Sanfaçon, H. (2007) Recovery of Nicotiana benthamiana plants from a necrotic response induced by a nepovirus is associated with RNA silencing but not with reduced virus titer J. Virol. 81, 12285-12297
Chisholm, J., Zhang, G., Wang, A. and Sanfaçon, H. (2007) Peripheral association of a polyprotein precursor form of the RNA-dependent RNA polymerase of Tomato ringspot virus with the membrane-bound viral replication complex.Virology 368, 133-144
Zhang G. and Sanfaçon, H. (2006) Characterization of membrane-association domains within the Tomato ringspot nepovirus X2 protein, an endoplasmic reticulum-targeted polytopic membrane protein. J. Virol. 80, 10847-10857
Zhang, S. C., Zhang, G., Yang, L, Chisholm, J. and Sanfaçon, H (2005). Evidence that insertion of Tomato ringspot virus NTB-VPg protein in endoplasmic reticulum membranes is controlled by two domains: a C-terminal transmembrane helix and an N-terminal amphipathic helix. J. Virol. 79, 11766-11775
Wang, A., Han, S. and Sanfaçon, H. (2004). Topogenesis in membranes of the NTB-VPg protein of Tomato ringspot nepovirus: definition of the C-terminal transmembrane domain. J. Gen. Virol. 85, 535-545
Han, S. and Sanfaçon, H. (2003). Tomato ringspot virus proteins containing the nucleoside triphosphate binding domain are transmembrane proteins that associate with the endoplasmic reticulum and co-fractionate with replication complexes. J. Virol. 77, 523-534
Léonard, S., Chisholm, J., Laliberté, J.F. and Sanfaçon, H. (2002). Interaction in vitro between the proteinase ofTomato ringspot virus (genus nepovirus) and the eukaryotic translation initiation factor iso4E from Arabidopsis thaliana. J. Gen. Virol. 83, 2085-2089