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Persistent Viral Diseases
 Neuroimmunology Unit
 Retroviral Immunology
 Retroviral Molecular Biology
 Retroviral Neuropathogenesis
 TSE/Prion Biochemistry
 TSE/Prion Cell Biology
 TSE/Prion Molecular Biology
 TSE/Prion and Retroviral Pathogenesis
 Veterinary Biology


Laboratory of Persistent Viral Diseases

Bruce W. Chesebro, M.D.

Chief, Laboratory of Persistent Viral Diseases
Chief, TSE/Prion and Retroviral Pathogenesis Section

TSE/Prion and Retroviral Pathogenesis

Dr. Chesebro received his M.D. from Harvard Medical School in 1968. He completed postdoctoral studies at Karolinska Institute, 1967; Stanford University, 1968-1970; and National Institute of Arthritis and Metabolic Diseases, 1970-1972. He came to the Rocky Mountain Laboratories in 1972 and became the chief of the Laboratory of Persistent Viral Diseases in 1979.

Figure shows protease-resistant prion protein (PrP-res) deposited as amyloid stained with Thioflavin S in the corpus callosum and cerebellum of an anchorless PrP transgenic mouse 194 days after infection with scrapie strain 22L.
Figure shows protease-resistant prion protein (PrP-res) deposited as amyloid stained with Thioflavin S in the corpus callosum and cerebellum of an anchorless PrP transgenic mouse 194 days after infection with scrapie strain 22L. Adapted from Chesebro et al. Science 308:1435-39, 2005.

Description of Research Program

Research is aimed at studying the pathogenesis of transmissible encephalopathies or prion diseases as well as murine and human retroviral diseases of the brain. These diseases are being studied at the biochemical, cellular, and whole animal model levels. Mutant prion protein (PrP) molecules have been expressed in neural cell cultures and in transgenic mice to study the effects of PrP alterations on agent replication and disease development. Knockout mice that lack expression of important cytokine and chemokine genes and their receptors are also used for pathogenesis studies. Similar approaches have been used for retroviral envelope mutants, which differ in their pathogenic properties.

Recently, together with collaborators at the Scripps Research Institute in La Jolla, our group developed a transgenic mouse model expressing anchorless prion protein. This model replicated the prion/TSE agent and has extensive amyloid deposits in the brain, but develops minimal clinical disease. This model has become an interesting new tool for studies of prion disease pathogenesis.

Research Group Members

James Striebel, M.S., Biologist; Mikael Klingeborn, Ph.D., Visiting Fellow; Deborah Tribouillard, Ph.D., Visiting Fellow; Brent Race, D.V.M., Veterinary Staff Scientist; Kimberly Meade-White, M.S., Biologist; Melissa Pathmajeyan, Graduate Student.

Selected Publications

(View list in PubMed)

LaCasse RA, Striebel JF, Favara C, Kercher L, Chesebro B. Role of Erk1/2 activation in prion disease pathogenesis: Absence of CCR1 leads to increased Erk1/2 activation and accelerated disease progression. J Neuroimmunol. 2008 Apr 5.

Kercher L, Favara C, Striebel JF, LaCasse R, Chesebro B. Prion protein expression differences in microglia and astroglia influence scrapie-induced neurodegeneration in the retina and brain of transgenic mice. J Virol. 2007 Oct;81(19):10340-51.

Meade-White K, Race B, Trifilo M, Bossers A, Favara C, Lacasse R, Miller M, Williams E, Oldstone M, Race R, Chesebro B. Resistance to chronic wasting disease in transgenic mice expressing a naturally occurring allelic variant of deer prion protein. J Virol. 2007 May;81(9):4533-9.

Trifilo MJ, Yajima T, Gu Y, Dalton N, Peterson KL, Race RE, Meade-White K, Portis JL, Masliah E, Knowlton KU, Chesebro B, Oldstone MB. Prion-induced amyloid heart disease with high blood infectivity in transgenic mice. Science. 2006 Jul 7;313(5783):94-7.

Peterson KE, Chesebro B. Influence of proinflammatory cytokines and chemokines on the neuropathogenesis of oncornavirus and immunosuppressive lentivirus infections. Curr Top Microbiol Immunol. 2006;303:67-95.

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.

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Photo of Bruce W. Chesebro, M.D.

Contact Info

Bruce W. Chesebro, M.D.
Phone: 406-363-9354
Fax: 406-363-9286
E-mail:
bchesebro@niaid.nih.gov

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  • Division of Intramural Research (DIR)
  • Training Resources

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    Photo of Bruce W. Chesebro, M.D.

    Contact Info

    Bruce W. Chesebro, M.D.
    Phone: 406-363-9354
    Fax: 406-363-9286
    E-mail:
    bchesebro@niaid.nih.gov

    See Also

  • Division of Intramural Research (DIR)
  • Training Resources