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Bessen Lab

Summary:

My laboratory is investigating agent-host interactions in prion diseases, which are fatal neurodegenerative diseases. These are important diseases of humans (Creutzfeldt-Jakob disease), livestock (e.g., scrapie in sheep and bovine spongiform encephalopathy in cattle) and cervids (chronic wasting disease) that have zoonotic potential. Although the majority of prion diseases are due to infection with the prion agent, they can also occur sporadically or as a result of an autosomal dominant mutation in the prion protein gene. The prion agent appears to be devoid of a nucleic acid genome and consists of a misfolded host protein, called PrP-res, that can further induce its own formation from the normal host prion protein. The multiple etiologies of prion diseases and the unusual nature of the infectious agent is novel in microbiology.

Research projects in the Bessen lab include investigations of (1) the routes of prion neuroinvasion following oral exposure; (2) the mechanism of prion agent entry and spread in nerve cells and skeletal muscle; (3) the host physiological responses during chronic wasting disease infection; and (4) transgenic models of CWD pathogenesis. Currently, there are postdoctoral and technical positions as well as graduate student openings available in the laboratory to pursue these studies.

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Instruments

Organisms and Viruses

  • F-ABCA1-Luciferase ( Lentivirus )

    Insert description: Luciferase linked to CD8 marker (lacking cytoplasmic domain) for FACS based selection of reporter cells.

  • LXSN-IkBaM ( Virus )

    Moloney virus; Insert description: transdominant negative I kappa B alpha (serine and threonine to alanine mutations at amino and carboxy terminus).

  • pCLMIG/Cre-W ( Virus )

    Insert description: GFP-Cre recombinase fusion protein with WPRE RNA stabilizing sequence.

  • pCLMTAg-IRES-bcl2-W ( Virus )

    Insert description: SV40 T antigen with IRES linked expression to human Bcl-2

  • pLXSN - Fas/TNFR1 ( Murine leukemia virus )

    Insert description: Fas extracellular, TNFRI cytoplasmic domain

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Last updated: 2011-04-27T16:00:03.733-05:00

Copyright © 2016 by the President and Fellows of Harvard College
The eagle-i Consortium is supported by NIH Grant #5U24RR029825-02 / Copyright 2016