To be fair, this doesn't have to have originated via animal-to-animal infection, but could be an example of sporadic CWD.
As far as I know, sporadic CWD is relatively uncommon, but given CWD is caused by the PrP protein, and there are a number of known mutations in PrP which can increase its likelihood of undergoing prion-conversion, I'd hope they're going to sequence this animal's PrP gene to see it it shed's some light on the etiology.
Irrespective, this could still mean that CWD is now endemic in Europe.
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Updated for clarity and extra info/context (thanks pbhjpbhj!)
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CWD: Chronic Wasting Disease (deer-based prion disease - main topic of article)
PrP: The specific prion protein involved here. Note that (confusingly!) prions are both a 'class' of proteins but also refers to a specific protein (PrP).
Prions (class) are proteins which can exist in one of two states. In their soluble form they're happy-go-lucky proteins that are monomeric (i.e. exist as a single unit). However, these soluble-form prions can undergo a conformational change (re-arrange their shape) into a different conformation (the infectious form). The infectious form of the prion can do two specific things: 1) Aggregate (so all the previous soluble prion proteins get stuck into a big wad of protein) 2): Catalyze the conversion of soluble-form prion into the infectious form. Herein lies their infectivity - you get an exponential growth in the number of proteins in the infectious state.
Prions (PrP) is a specific protein found in many higher-order multicellular organisms that is the SPECIFIC protein that causes a range of prion diseases (Creutzfeldt-Jakob Disease (CJD), BSE [mad cow], CWD, Scrapie etc). There are species barriers to these diseases, even though the proteins are pretty similar (i.e. humans cannot catch CWD from deer, even though the PrP protein misfolds in CWD and the same human version misfolds in CJD). These species barriers are convenient (!!) but very poorly understood, which is somewhat concerning.
Finally - it's worth point out prions aren't always bad. Fungi use them as a mechanism to facilitate non-genetic heritability/diversity [1], and we're increasingly finding examples of prion-like mechanisms that facilitate fast and irreversible signalling in cells (e.g. in the inflammation response [2])
[1] True, H. L. & Lindquist, S. L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407, 477–483 (2000).
[2] Cai, X. et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell 156, 1207–1222 (2014).
As far as I know, sporadic CWD is relatively uncommon, but given CWD is caused by the PrP protein, and there are a number of known mutations in PrP which can increase its likelihood of undergoing prion-conversion, I'd hope they're going to sequence this animal's PrP gene to see it it shed's some light on the etiology.
Irrespective, this could still mean that CWD is now endemic in Europe.
>>>
Updated for clarity and extra info/context (thanks pbhjpbhj!)
>>>
CWD: Chronic Wasting Disease (deer-based prion disease - main topic of article)
PrP: The specific prion protein involved here. Note that (confusingly!) prions are both a 'class' of proteins but also refers to a specific protein (PrP).
Prions (class) are proteins which can exist in one of two states. In their soluble form they're happy-go-lucky proteins that are monomeric (i.e. exist as a single unit). However, these soluble-form prions can undergo a conformational change (re-arrange their shape) into a different conformation (the infectious form). The infectious form of the prion can do two specific things: 1) Aggregate (so all the previous soluble prion proteins get stuck into a big wad of protein) 2): Catalyze the conversion of soluble-form prion into the infectious form. Herein lies their infectivity - you get an exponential growth in the number of proteins in the infectious state.
Prions (PrP) is a specific protein found in many higher-order multicellular organisms that is the SPECIFIC protein that causes a range of prion diseases (Creutzfeldt-Jakob Disease (CJD), BSE [mad cow], CWD, Scrapie etc). There are species barriers to these diseases, even though the proteins are pretty similar (i.e. humans cannot catch CWD from deer, even though the PrP protein misfolds in CWD and the same human version misfolds in CJD). These species barriers are convenient (!!) but very poorly understood, which is somewhat concerning.
Finally - it's worth point out prions aren't always bad. Fungi use them as a mechanism to facilitate non-genetic heritability/diversity [1], and we're increasingly finding examples of prion-like mechanisms that facilitate fast and irreversible signalling in cells (e.g. in the inflammation response [2])
[1] True, H. L. & Lindquist, S. L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407, 477–483 (2000).
[2] Cai, X. et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell 156, 1207–1222 (2014).