NDLI: Prion Transmission Prevented by Modifying the β2-α2 Loop Structure of Host PrPC

Content Provider	PubMed Central
Author	Kurt, Timothy D. Bett, Cyrus Natalia, Fernández-borges Joshi-barr, Shivanjali Hornemann, Simone Thomas, Rülicke Castilla, Joaquín Wüthrich, Kurt Adriano, Aguzzi Sigurdson, Christina J.
Copyright Year	2014
Abstract	Zoonotic prion transmission was reported after the bovine spongiform encephalopathy (BSE) epidemic, when >200 cases of prion disease in humans were diagnosed as variant Creutzfeldt-Jakob disease. Assessing the risk of cross-species prion transmission remains challenging. We and others have studied how specific amino acid residue differences between species impact prion conversion and have found that the β2-α2 loop region of the mouse prion protein (residues 165–175) markedly influences infection by sheep scrapie, BSE, mouse-adapted scrapie, deer chronic wasting disease, and hamster-adapted scrapie prions. The tyrosine residue at position 169 is strictly conserved among mammals and an aromatic side chain in this position is essential to maintain a 310-helical turn in the β2-α2 loop. Here we examined the impact of the Y169G substitution together with the previously described S170N, N174T “rigid loop” substitutions on cross-species prion transmission in vivo and in vitro. We found that transgenic mice expressing mouse PrP containing the triple-amino acid substitution completely resisted infection with two strains of mouse prions and with deer chronic wasting disease prions. These studies indicate that Y169 is important for prion formation, and they provide a strong indication that variation of the β2-α2 loop structure can modulate interspecies prion transmission.
Related Links	http://dx.doi.org/10.1523/jneurosci.4636-13.2014
Ending Page	1027
Page Count	6
Starting Page	1022
File Format	PDF
ISSN	02706474
e-ISSN	15292401
Journal	The Journal of Neuroscience
Issue Number	3
Volume Number	34
Language	English
Publisher	Society for Neuroscience
Publisher Date	2014-01-15
Access Restriction	Open
Rights Holder	Society for Neuroscience
Subject Keyword	Neuroscience(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience

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