Bruce W. Chesebro, M.D.

Senior Investigator

TSE / Prion and Retroviral Pathogenesis Section


Rocky Mountain Laboratories
Building 3, Room 3203
903 South 4th Street
Hamilton, MT 59840


Research Topics

Research is aimed at studying the pathogenesis of transmissible encephalopathies or prion diseases. These diseases are being studied at the biochemical, cellular, and whole animal model levels. We are currently studying both chronic wasting disease (CWD) of deer and elk as well as rodent-adapted sheep scrapie. Rodent and nonhuman primate models are being used for CWD. 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.

Our group also studies a transgenic mouse model expressing anchorless prion protein. This model replicates the prion/TSE agent and has extensive amyloid deposits in the brain with cerebral amyloid angiopathy similar to human brain amyloid diseases including Alzheimer’s disease. This model mimics a new fatal familial prion disease in which patients express prion protein with a stop codon near the C-terminus, thus eliminating the GPI anchoring of prion protein.


Dr. Chesebro received his M.D. from Harvard Medical School in 1968. He completed postdoctoral studies at the Karolinska Institute, Sweden, in 1967; at Stanford University from 1968 to 1970; and at the National Institute of Arthritis and Metabolic Diseases from 1970 to 1972. He came to NIAID in 1972 and became chief of the Laboratory of Persistent Viral Diseases in 1979. Elected as a Fellow in the American Academy of Microbiology, 2011.

Selected Publications

  1. Chesebro B, Race B, Meade-White K, Lacasse R, Race R, Klingeborn M, Striebel J, Dorward D, McGovern G, Jeffrey M. Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring. PLoS Pathog. 2010;6(3):e1000800.

  2. Klingeborn M, Race B, Meade-White KD, Chesebro B. Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions. Proc Natl Acad Sci U S A. 2011;108(48):E1244-53.

  3. Chesebro B, Striebel J, Rangel A, Phillips K, Hughson A, Caughey B, Race B. Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice. MBio. 2015;6(5):e01419-15.

  4. Carroll JA, Striebel JF, Rangel A, Woods T, Phillips K, Peterson KE, Race B, Chesebro B. Prion Strain Differences in Accumulation of PrPSc on Neurons and Glia Are Associated with Similar Expression Profiles of Neuroinflammatory Genes: Comparison of Three Prion Strains. PLoS Pathog. 2016;12(4):e1005551.

  5. Klingeborn M, Race B, Meade-White KD, Rosenke R, Striebel JF, Chesebro B. Crucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infection. J Virol. 2011;85(4):1484-94.

This page was last updated on April 24th, 2018