Perspective on what the novel CWD prion structure means for the prion field
🧠 A new Open Access review by Szymon W. Manka, published in JNC, explores a major step forward in prion research.
Until now, most structural studies focused on rodent-adapted scrapie strains. This review highlights the first prion structure identified from a naturally occurring case of Chronic Wasting Disease (CWD) in deer, offering fresh insight into how prion proteins misfold in different species.
What does this mean for the field? The findings suggest that species-specific prion structures may help explain interspecies transmission barriers, and why some prions stay contained while others may pose broader risks.
🔗🔓Read the full article here: https://lnkd.in/dK66GEdw
Graphical abstract
The normal prion protein (PrPC) fold is shared among mammals; however, it can undergo misfolding in various ways, giving rise to distinct infectious prion (PrPSc) strains. This review describes independent misfolding subdomains within PrP, recognised through new structural alignments and comparisons with the novel deer chronic wasting disease (CWD) prion structure. It shows that these conformationally independent segments support prion diversity, lacking any universally conserved conformational motifs across various host species. It further suggests that certain species-specific conformations may be implicated in interspecies prion transmission barriers.
