Education and Training:
B.Sc., Biochemistry, University of British Columbia, 1984-1988
Ph.D., Microbiology and Immunology, University of British Columbia, 1988-1994
Post-Doctoral Fellow, Microbiology and Immunology, University of British Columbia, 1994-1996
Visiting Research Fellow, Molecular Biology, Princeton University, 1996-1999
Assistant Professor, Department of Microbiology, University of Colorado Health Sciences Center, 1999
Associate Professor, Department of Microbiology, University of Colorado Health Sciences Center, 2006
Associate Professor, Department of Microbiology and Immunology, Queen's University, 2007
Professor, Department of Biomedical and Molecular Sciences, Queen's University, 2013
Canadian Institutes of Health Research, Project Grant, "Early stages in the morphogenesis of herpes simplex virus"
Natural Science and Engineering Council of Canada, Discovery Grant, "Remodeling of the nuclear membrane during herpesvirus assembly"
Viruses are selective and efficient nucleic acid delivery devices that serve as excellent tools for studying complex macromolecular assemblies as well as core cellular functions. The order Herpesvirales is a very large group of viruses that infect animals ranging from oysters to elephants. The model herpesvirus studied in the Banfield laboratory is the important human pathogen, herpes simplex virus type 2 (HSV-2), a large virus encoding 74 distinct proteins. HSV-2 virions are complex machines containing almost 100 different proteins. Approximately half of these structural proteins are encoded by the viral genome and the other half are of cellular origin. All herpes virions share a layered structure: a linear double-stranded DNA genome encased by an icosahedral nucleocapsid, which is surrounded by a lipid envelope embedded with glycoproteins. Between the nucleocapsid and the envelope lies a proteinaceous layer called the tegument. During infection, the virion nucleocapsid and tegument components enter the cell cytoplasm. The tegument proteins delivered into the cytoplasm during infection have the opportunity to perform a variety of functions prior to new virus gene expression. A widely held view is that a key role for incoming tegument proteins is to establish an environment within the cell that is conducive to virus replication. In keeping with this view, our research focuses on the analysis of several viral tegument proteins and how they counteract different intrinsic cellular antiviral defense mechanisms aimed at restricting the production of new viruses. Additionally, many tegument proteins play fundamental roles in virus assembly and mediate the release of newly formed virions from the cell. Our laboratory is actively engaged in determining the role of tegument components in the assembly and release of herpesvirus virions from infected cells.
Finnen RL, BB Roy, H Zhang and BW Banfield. 2010. “Analysis of filamentous process induction and nuclear localization properties of the HSV-2 serine/threonine kinase Us3”. Virology 397: 23-33.
Babic T, MN Purpera, BW Banfield, HR Berthoud and CD Morrison. 2010. “Innervation of skeletal muscle by leptin receptor-containing neurons” Brain Res.1345:146-55
Finnen RL and BW Banfield, 2010. “Subcellular localization of the alphaherpesvirus serine/threonine kinase Us3 as a determinant of Us3 function”. Virulence. 1:291-294.
Kang MH and BW Banfield. 2010. “Pseudorabies virus tegument protein Us2 recruits the mitogen-activated protein kinase extracellular-regulated kinase (ERK) to membranes through interaction with the ERK common docking domain”. J. Virol. 84:8395-8408.
Walters MS, PR Kinchington, BW Banfield and S Silverstein. 2010. “Hyperphosphorylation of histone deacetylase 2 by alphaherpesvirus Us3 kinases”. J. Virol. 84:9666-9676.
Erazo A, MB Yee, BW Banfield and PR Kinchington. 2011. “The alphaherpesvirus Us3/ORF66 protein kinases direct phosphorylation of the nuclear matrix protein matrin 3”. J. Virol. 85:568-581
Jung M, RL Finnen, CE Neron and BW Banfield. 2011.”The alphaherpesvirus serine/threonine kinase Us3 disrupts PML nuclear bodies”. J. Virol. 85:5301-5311
Finnen RL, SM Johnston, CE Neron and BW Banfield. 2011. “Nucleocytoplasmic shuttling of the HSV-2 serine/threonine kinase Us3”. Virology. 417:229-237.
Guzzo, C, A Ayer, S. Basta, BW Banfield and K Gee. 2012. “IL-27 enhances LPS-induced pro-inflammatory cytokine production via upregulation of TLR-4 expression and signaling in human monocytes". J. Immunol.188:864-873.
Finnen RL, KR Pangka and BW Banfield. 2012. “Herpes simplex virus 2 infection impacts stress granule accumulation”. J. Virol. 86:8119-8130.
Le Sage V and BW Banfield. 2012. “Dysregulation of autophagy in murine fibroblasts resistant to HSV-1 infection”. PLoS One. 7(8):e42636
Guzzo C, M Jung, A Graveline, BW Banfield and K Gee. 2012 “IL-27 increases BST-2 expression in human monocytes and T cells”. Sci Rep. 2:974.
Le Sage V, M Jung, JD Alter, EG Wills, SM Johnston, Y Kawaguchi, JD Baines and BW Banfield. 2013. “The herpes simplex virus type 2 UL21 protein is essential for virus propagation”. J. Virol. 87:5904-5915.
Kang MH, BB Roy, RL, Finnen , V Le Sage, SM Johnston, H Zhang and BW Banfield. 2013. “The Us2 gene product of herpes simplex virus 2 is a membrane associated ubiquitin binding protein”. J. Virol.87:9590-9603
Nguyen, NLT, J. Randall, BW Banfield and TJ Bartness. 2014. “Central sympathetic innervations to visceral and subcutaneous white adipose tissue”. Am J Physiol Regul Integr Comp Physiol.306:R375-86. PMID:24452544.
Finnen RL, TJ Hay, B Dauber, JR Smiley and BW Banfield. 2014. “The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation”. J.Virol.88:12727-12739.
Banfield BW, AJ Mouland and C McCormick. 2014. “1st International symposium on stress-associated RNA granules in human disease and viral infection”. Viruses 6:3500-3513.
Finnen RL, M Zhu, J Li, D Romo and BW Banfield. 2016 “Herpes simplex virus 2 virion host shutoff endoribonuclease activity is required to disrupt stress granule formation”. J.Virol.90:7943-7955.
Finnen RL and BW Banfield. 2016. “Alphaherpesvirus subversion of stress-induced translational arrest”. Viruses. 8:81
Gao J, TJM Hay and BW Banfield. 2017. “The product of the herpes simplex virus type 2 UL16 gene is critical for the egress of capsids from the nuclei of infected cells”. J.Virol. 91:e00350-17.
Petes C, C Wynick, C Guzzo, D Mehta, S Logan, BW Banfield, S Basta, A Cooper and K Gee. 2017. “IL-27 enhances LPS-induced IL-1beta in human monocytes and murine macrophages”. J. Leukoc. Biol. 102(1):83-94
Sherry MR, TJM Hay, MA Gulak, A Nassiri, RL Finnen and BW Banfield. 2017. “The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding”. Sci.Rep. 7(1):1882.
Gao J, X Yan and BW Banfield. 2018. “Comparative Analysis of UL16 Mutants Derived from Multiple Strains of HSV-2 and HSV-1 Reveals Species-Specific Requirements for the UL16 Protein”. J. Virol. 92. PMID:29669832
Finnen RL and BW Banfield. 2018. "CRISPR/Cas9 Mutagenesis of UL21 in Multiple Strains of Herpes Simplex Virus Reveals Differential Requirements for pUL21 in Viral Replication". Viruses. PMID:29762484
Petes C, V Mintsopoulos, RL Finnen, BW Banfield and K Gee. 2018. "The effects of CD14 and IL-27 on induction of endotoxin tolerance in human monocytes and macrophages". J Biol Chem. PMID:30242126
Banfield BW. 2019. "Beyond the NEC: modulation of herpes simplex virus nuclear egress by viral and cellular components." Curr Clin Micro Rpt. https://doi.org/10.1007/s40588-019-0112-7