Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Prion transmission prevented by modifying the beta 2-alpha 2 loop structure of host PrP(C)

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Kurt, T. D.
  • Bett, C.
  • Fernandez-Borges, N.
  • Joshi-Barr, S.
  • Hornemann, S.
  • Rulicke, T.
  • Castilla, J.
  • Wuthrich, Kurt
  • Aguzzi, A.
  • Sigurdson, Christina

publication date

  • January 2014

journal

  • Journal of Neuroscience  Journal

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.

subject areas

  • Amino Acid Substitution
  • Animals
  • Cattle
  • Cricetinae
  • Deer
  • Female
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Prion Diseases
  • Prions
  • Protein Structure, Secondary
  • Sheep
  • Species Specificity
scroll to property group menus

Research

keywords

  • TSE
  • amyloid
  • conversion
  • prions
  • transmission
scroll to property group menus

Identity

PubMed Central ID

  • PMC3891945

International Standard Serial Number (ISSN)

  • 0270-6474

Digital Object Identifier (DOI)

  • 10.1523/jneurosci.4636-13.2014

PubMed ID

  • 24431459
scroll to property group menus

Additional Document Info

start page

  • 1022

end page

  • 1027

volume

  • 34

issue

  • 3

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support