Glynn, Calina
Callie is a graduate student in the Biochemistry, Molecular and Structural Biology Program. She received a B.A. degree from Boston University in 2016, and then came to UCLA and joined the laboratory of Dr. Jose Rodriguez. She entered the CMB Training Program in 2017.
Mentor: Dr. Jose Rodriguez
Nearly two dozen protein misfolding diseases have been named to date, each associated with misfolding, and often accumulation, of a particular protein. These include Alzheimers, Parkinsons, and type II diabetes, among others. Also belonging to this family are prion diseases, whereby the prion protein (PrP) is uniquely able to self-propagate its infectious state (PrPsc) by inducing a conformational change on its native cellular state to confer disease without any genetic abnormality.
Prion disease is transmitted between species by overcoming what is known as the “species barrier”, a physiological or molecular limitation preventing the spread of infectious prions from one species to another. The species barrier is not constant for prion. Minor differences in sequence may account for this variability; however, there is no molecular explanation for the incongruent efficiency of prion spread between species. This creates a problem that is best addressed from a structural, rather than simply genetic, vantage point. I perform systematic analyses of differences in PrPsc structure across mammals to provide a more complete picture of what is holding structures together and what common patterns are required for disease transfer between distinct subsets of species. These comparisons could predict risk of transfer between pairs of species whose disease transfer capacity has not been studied in vivo.
