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Suggested Citation:"Color Plates." Institute of Medicine. 2004. Advancing Prion Science: Guidance for the National Prion Research Program. Washington, DC: The National Academies Press. doi: 10.17226/10862.
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Page 259
Suggested Citation:"Color Plates." Institute of Medicine. 2004. Advancing Prion Science: Guidance for the National Prion Research Program. Washington, DC: The National Academies Press. doi: 10.17226/10862.
×
Page 260
Suggested Citation:"Color Plates." Institute of Medicine. 2004. Advancing Prion Science: Guidance for the National Prion Research Program. Washington, DC: The National Academies Press. doi: 10.17226/10862.
×
Page 261
Suggested Citation:"Color Plates." Institute of Medicine. 2004. Advancing Prion Science: Guidance for the National Prion Research Program. Washington, DC: The National Academies Press. doi: 10.17226/10862.
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Page 262

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PLATE 2-1 Depiction of the three-dimensional structure of the intact human prion protein, PrP (23-230~. The a-helices are orange, the p-sheets blue. The segments with nonregular secondary structure within the C-te'lllinal domain are yellow. Yellow dots represent the flexibly disordered tail composed of residues 23-121. Reprinted from Zahn et al. (2000) with permission from Proceedings of the National Academy of the United States (2000~. Copyright 2000, Proceedings of the National Academy of the United States.

b. ... is, ~~.~ Phi Ad_ , .~ PLATE 2-2 Hypothetical models of PrP 27-30, the pro/ease-resistant segment of PrPSc. (a) Three PrP 27-30 polypeptide models scaled and positioned to reflect the presumed structure of the crystal in the background. Each polypeptide has three p- sheet regions (blue) and two a-helices (red). The background is an electron micrograph of a two-dimensional crystal of PrP 27-30 after image processing. (b) A side view of the hypothesized structure of a short segment of a scrapie-associated fibril. Multiple sets of PrP 27-30 polypeptide trimers, viewed from above in (a), are stacked here to form part of a rod-shaped fibril. SOURCES: electron micrograph: H. Wille, Institute for Neurodegenerative Diseases, University of California, San Francisco, July 2003; models: C. Govaerts, Department of Cellular and Molecular Pharmacology, University of California, San Francisco, July 2003.

Normal sCJ :) vCUD PLATE 4-1 The results of hematoxylin and eosin (HOE) staining (top row) and of immunohistochemical staining (IHC) of PrP (bottom row) are visible in microphotography of human brain tissue from a normal brain, the brain of a patient with sCID, and the brain of a patient with vCID. Top row: The white spaces in sCTD and vCID tissue are vacuoles, a sign of neurodegeneration described as spongiform. In sCTD, the vacuoles are minute and evenly distributed; by contrast, in vCID, they are relatively large and mainly clustered around plaques in formations commonly called florid plaques or daisy plaques the hallmark of vCID. Bottom row: The IHC technique used on these tissues stains PrP brown and removes PrPC, hence the absence of staining in normal tissue. The fine, ubiquitous brown stain in sCID tissue indicates a fairly even distribution of PrPSC, whereas the spotty, intense brown stains in vCJD tissue reflect an uneven distribution of the protein, whichhas accumulated in plaques. SOURCE: I. Ironside, National CID Surveillance Center, Edinburgh, and P. Gambetti, National Prion Disease Pathology Surveillance Center, Cleveland, Ohio, September 2003.

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In Advancing Prion Science, the Institute of Medicine’s Committee on Transmissible Spongiform Encephalopathies Assessment of Relevant Science recommends priorities for research and investment to the Department of Defense’s National Prion Research Program (NPRP). Transmissible spongiform encephalopathies (TSEs), also called prion diseases, are invariably fatal neurodegenerative infectious diseases that include bovine spongiform encephalopathy (commonly called mad cow disease), chronic wasting disease, scrapie, and Creutzfeldt-Jakob disease. To develop antemortem diagnostics or therapies for TSEs, the committee concludes that NPRP should invest in basic research specifically to elucidate the structural features of prions, the molecular mechanisms of prion replication, the mechanisms of TSE pathogenesis, and the physiological function of prions’ normal cellular isoform. Advancing Prion Science provides the first comprehensive reference on present knowledge about all aspects of TSEs—from basic science to the U.S. research infrastructure, from diagnostics to surveillance, and from prevention to treatment.

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