Dr. Christina Sigurdson received her DVM at the University of California, Davis in 1994 and a PhD funded by an NIH fellowship at Colorado State University (CSU) in 2001. In 2002, she completed an anatomic pathology residency at CSU and became a Diplomat of the American College of Veterinary Pathologists. She then pursued postdoctoral studies of prion diseases at the University of Zürich, Switzerland with an award from the US Department of Defense. In 2008, Dr. Sigurdson joined the faculty at the University of California at San Diego and at Davis. Dr. Sigurdson has served as a scientific advisor in European Union committees as well as participated in international scientific meetings on protein misfolding disorders.

We are interested in the molecular pathogenesis of transmissible spongiform encephalopathies (TSEs), a family of fatal neurodegenerative disorders of humans and animals that includes Creutzfeldt-Jakob disease (CJD), bovine spongiform encephalopathy (BSE) or “mad cow disease”, and chronic wasting disease (CWD) of cervids. An essential component of the infectious agent is a misfolded, beta-sheet rich conformer of the cellular prion protein, thus the TSEs are also called prion diseases.

We are studying both the genetic and the environmental factors that influence prion transmission. Recently, we showed that mastitis can induce pathogenic prions to accumulate in the mammary gland. We are now exploring whether this environmental factor can enhance the transmission of prion disease via prion shedding into the milk. We are also investigating mutations in the prion gene that enable or inhibit prion transmission between species.

A third research focus is based on how the cellular prion protein structure may predispose to prion disease development. To this end, we have developed a transgenic mouse expressing a stucturally defined mutant prion protein. This mouse develops de novo prion disease, with prion aggregates and spongiform lesions in the brain, and may provide insights into the mechanisms of neurodegeneration and potential therapies to arrest a prion infection.