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© Valérie Choumet
Mosquitoes were orally infected with the chikungunya virus. Midguts were dissected at day 5 post-infection, fixed and permeabilised. Virus is shown in red (anti-E2 protein, cyanine 3), the actin network in green (phalloidin 548) and nuclei in blue (DAPI).
Publication : FEBS letters

Most of the structural elements of the globular domain of murine prion protein form fibrils with predominant beta-sheet structure

Team: Chemistry of Biomolecules
Team: Archived: Group: Françoise Baleux
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 01 Oct 2002

Jamin N, Coïc YM, Landon C, Ovtracht L, Baleux F, Neumann JM, Sanson A

Link to Pubmed [PMID] – 12372610

FEBS Lett. 2002 Oct;529(2-3):256-60

The conversion of the cellular prion protein into the beta-sheet-rich scrapie prion protein is thought to be the key step in the pathogenesis of prion diseases. To gain insight into this structural conversion, we analyzed the intrinsic structural propensity of the amino acid sequence of the murine prion C-terminal domain. For that purpose, this globular domain was dissected into its secondary structural elements and the structural propensity of the protein fragments was determined. Our results show that all these fragments, excepted that strictly encompassing helix 1, have a very high propensity to form structured aggregates with a dominant content of beta-sheet structures.