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Review
. 2017 Jul 6;13(7):e1006323.
doi: 10.1371/journal.ppat.1006323. eCollection 2017 Jul.

Prion strains in mammals: Different conformations leading to disease

Rodrigo Morales  1
Affiliations
Review

Prion strains in mammals: Different conformations leading to disease

Rodrigo Morales. PLoS Pathog. .
No abstract available

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Conflict of interest statement

The author has declared that no competing interests exist.

Figures

Fig 1
Fig 1. Differential biological and biochemical features used to distinguish between prion strains.
(A) Incubation periods to disease are one of main features allowing differentiation between prion isolates. Time differences between the incubation periods of 2 prion strains may vary depending on the route of administration. (B) Different clinical manifestations may also help to discriminate between different prion agents. This property has been very useful in some species (including goats and hamsters) but inefficient in others (such as mice). For example, signs as dissimilar as hyperactivity and hyperphagia can be observed within a single animal species (in this case, Syrian hamsters). (C) Prion isolates are known to induce spongiform degeneration in different areas of the brain in a strain-specific manner. Recently, similar profiles have been adapted for the disease-associated prion protein (PrPSc) deposition as well. In this graphic example, darker color in certain brain areas represents more severe damage. (D) At the molecular level, the partial proteolytic resistance of PrPSc lies in its C-terminal region. Strain-specific prion folding is thought to protect different lengths of the polypeptide chain from proteases, leading to different electrophoretic mobilities. In this western blot model, no–Proteinase K treated cellular prion protein (PrPC) is shown as comparison (black). (E) The ability of certain prion arrangements to recruit specific PrP glycoforms also helps with easy strain characterization by western blots. (F) Resistance to proteolytic degradation by increasing the concentration of proteases is commonly used to investigate the identity of putatively different prion isolates.
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