Shadoo binds lipid membranes and undergoes aggregation and fibrillization

Biochemical and Biophysical Research Communications

Volumn 438, Issue 3, 2013, Pages 519-525

  Li, Qiaojing ^a   Chevalier, Christophe ^a   Henry, Céline ^b   Richard, Charles Adrien ^a   Moudjou, Mohammed ^a   Vidic, Jasmina ^a  

^a INRA Institut National de la Recherche Agronomique   (France)

^b CEMAGREF   (France)

Author keywords

Amyloid fibers; Circular dichroism; Electron microscopy; Lipid membrane; Membrane perturbation; Shadoo

Indexed keywords

AMYLOID; LIPOSOME; PRION PROTEIN; SHADOO PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DISEASE ASSOCIATION; LIPID BILAYER; LIPID MEMBRANE; LIPID VESICLE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN FIBRILLIZATION; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTEIN PROCESSING;

AMYLOID FIBERS; CIRCULAR DICHROISM; ELECTRON MICROSCOPY; LIPID-MEMBRANE; MEMBRANE PERTURBATION; SHADOO;

AMYLOID; LIPID BILAYERS; LIPOSOMES; MEMBRANE LIPIDS; NERVE TISSUE PROTEINS; PRION DISEASES;

EID: 84882821859     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.07.104     Document Type: Article

References (18)

1. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 1982, 216:136-144.
2. Prusiner S.B., McKinley M.P., Bowman K.A., Bolton D.C., Bendheim P.E., Groth D.F., Glenner G.G. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 1983, 35:349-358.
3. Kraus A., Groveman B.R., Caughey B. Prions and the potential transmissibility of protein misfolding diseases. Annu. Rev. Microbiol. 2013, 67:543-564.
4. Walmsley A.R., Zeng F., Hooper N.M. The N-terminal region of the prion protein ectodomain contains a lipid raft targeting determinant. J. Biol. Chem. 2003, 278:37241-37248.
5. Steunou S., Chich J.F., Rezaei H., Vidic J. Biosensing of lipid-prion interactions: insights on charge effect, Cu(II)-ions binding and prion oligomerization. Biosens. Bioelectron. 2010, 26:1399-1406.
6. Borchelt D.R., Taraboulos A., Prusiner S.B. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 1992, 267:16188-16199.
7. Westaway D., Daude N., Wohlgemuth S., Harrison P. The PrP-like proteins Shadoo and Doppel. Top Curr. Chem. 2011, 305:225-256.
8. Daude N., Ng V., Watts J.C., Genovesi S., Glaves J.P., Wohlgemuth S., Schmitt-Ulms G., Young H., McLaurin J., Fraser P.E., Westaway D. Wild-type Shadoo proteins convert to amyloid-like forms under native conditions. J. Neurochem. 2010, 113:92-104.
9. Watts J.C., Drisaldi B., Ng V., Yang J., Strome B., Horne P., Sy M.S., Yoong L., Young R., Mastrangelo P., Bergeron C., Fraser P.E., Carlson G.A., Mount H.T., Schmitt-Ulms G., Westaway D. The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections. EMBO J. 2007, 26:4038-4050.
10. Watts J.C., Stöhr J., Bhardwaj S., Wille H., Oehler A., Dearmond S.J., Giles K., Prusiner S.B. Protease-resistant prions selectively decrease Shadoo protein. PLoS Pathog. 2011, 7:e1002382.
11. Necula M., Chirita C.N., Kuret J. Rapid anionic micelle-mediated alpha-synucleinfibrillization in vitro. J. Biol. Chem. 2003, 278:46674-46680.
12. Domanov Y.A., Kinnunen P.K. Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers. J. Mol. Biol. 2008, 376:42-54.
13. Chirita C.N., Necula M., Kure J. Anionic micelles and vesicles induce tau fibrillization in vitro. J. Biol. Chem. 2003, 278:25644-25650.
14. Stefani M. Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity. FEBS J. 2010, 277:4602-4613.
15. Sanghera N., Swann M.J., Ronan G., Pinheiro T.J. Insight into early events in the aggregation of the prion protein on lipid, membranes. Biochim. Biophys. Acta 2009, 1788:2245-2251.
16. Zhao H., Jutila A., Nurminen T., Wickström S.A., Keski-Oja J., Kinnunen P.K. Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers. Biochemistry 2005, 44:2857-2863.
17. Gellermann G.P., Appel T.R., Tannert A., Radestock A., Hortschansky P., Schroeckh V., Leisner C., Lütkepohl T., Shtrasburg S., Röcken C., Pras M., Linke R.P., Diekmann S., Fändrich M. Raft lipids as common components of human extracellular amyloid fibrils. Proc. Natl. Acad. Sci. USA 2005, 102:6297-6302.
18. Westaway D., Genovesi S., Daude N., Brown R., Lau A., Lee I., Mays C.E., Coomaraswamy J., Canine B., Pitstick R., Herbst A., Yang J., Ko K.W., Schmitt-Ulms G., Dearmond S.J., McKenzie D., Hood L., Carlson G.A. Down-regulation of Shadoo in prion infections traces a pre-clinical event inversely related to PrP(Sc) accumulation. PLoS Pathog. 2011, 7:e1002391.