Bruce W Banfield, Ph.D

Bruce W Banfield

Faculty Bio

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.

Last Modified: 2014-10-02