title: Shadoo binds lipid membranes and undergoes aggregation and fibrillization.
abstract: Lipid membrane can enhance prion protein (PrP) pathological fibrillogenesis. A neuronal paralog of PrP, named Shadoo (Sho), is localized to similar membrane environment as PrP and can also convert to amyloid-like fibrilles. To gain insight into the role of Sho in prion diseases, we studied Sho interactions with cellular membrane models. Sho was found to bind anionic lipid vesicles. Spectroscopic and microscopic data showed that membrane-associated Sho slowly converted into amyloid fibers. Furthermore, binding of Sho to anionic liposomes has a disruptive effect on the integrity of the lipid bilayer leading to the formation of supramolecular lipid-protein complexes. In consequence, the role of Sho in prion diseases might depend on the oligomerization state of Sho but also the nature of these lipoprotein assembles.
authors.affiliation: Virologie et Immunologie Moléculaires - INRA, Jouy en Josas, France.
authors.forename: Qiaojing
authors.initials: Q
authors.lastname: Li
authors.forename: Christophe
authors.initials: C
authors.lastname: Chevalier
authors.forename: Céline
authors.initials: C
authors.lastname: Henry
authors.forename: Charles-Adrien
authors.initials: CA
authors.lastname: Richard
authors.forename: Mohammed
authors.initials: M
authors.lastname: Moudjou
authors.forename: Jasmina
authors.initials: J
authors.lastname: Vidic
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D058851:GPI-Linked Proteins; D008051:Lipid Bilayers / Q000378:metabolism; D008081:Liposomes / Q000378:metabolism*; D008563:Membrane Lipids / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D017096:Prion Diseases
chemical_list: D000682:Amyloid; D058851:GPI-Linked Proteins; D008051:Lipid Bilayers; D008081:Liposomes; D008563:Membrane Lipids; D009419:Nerve Tissue Proteins; C523856:Sprn protein, mouse
keywords: Amyloid fibers; Circular dichroism; Electron microscopy; Lipid-membrane; Membrane perturbation; Shadoo