Gerald S. Baron, Ph.D.

Chief, TSE/Prion Cell Biology Section
Investigator

Trafficking of fluorescent prions in a neuronal cell.

Dr. Baron received his Ph.D. in biochemistry from the University of Victoria in 1998, studying genes required for intramacrophage growth of the facultative intracellular bacterium, Francisella tularensis. He conducted his postdoctoral research on prions and transmissible spongiform encephalopathies (TSEs), in the laboratory of Dr. Byron Caughey at the Rocky Mountain Laboratories. In 2005, he established an independent laboratory as a tenure-track investigator.

Description of Research Program

TSEs or prion diseases are under investigation. TSEs are transmissible neurodegenerative disorders associated with the accumulation of a misfolded form of a host protein called PrP. Our work encompasses several areas, including determining mechanisms of infection, intra- and intercellular transport of TSE agents and neurodegeneration, in addition to defining the nature of the TSE agent. Biochemical and cell biological approaches in both cell culture and in vivo models of infection are being employed to address these questions.

Research Group Members

Yuzuru Taguchi, Jonathan Speare, Lindsay Hohsfield and Danielle Offerdahl

Selected Publications

(View list in PubMed.)

Baron GS, Magalhães AC, Prado MA, Caughey B. Mouse-adapted scrapie infection of SN56 cells: greater efficiency with microsome-associated versus purified PrP-res. J Virol. 2006 Mar;80(5):2106-17.

Magalhães AC, Baron GS, Lee KS, Steele-Mortimer O, Dorward D, Prado MA, Caughey B. Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells. J Neurosci. 2005 May 25;25(21):5207-16.

Chesebro B, Trifilo M, Race R, Meade-White K, Teng C, LaCasse R, Raymond L, Favara C, Baron G, Priola S, Caughey B, Masliah E, Oldstone M. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science. 2005 Jun 3;308(5727):1435-9.

Maxson L, Wong C, Herrmann LM, Caughey B, Baron GS. A solid-phase assay for identification of modulators of prion protein interactions. Anal Biochem. 2003 Dec 1;323(1):54-64.

Baron GS, Caughey B. Effect of glycosylphosphatidylinositol anchor-dependent and -independent prion protein association with model raft membranes on conversion to the protease-resistant isoform. J Biol Chem. 2003 Apr 25;278(17):14883-92.

Baron GS, Wehrly K, Dorward DW, Chesebro B, Caughey B. Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes. EMBO J. 2002 Mar 1;21(5):1031-40.

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