Thr but Asn of the N-glycosylation sites of PrP is indispensable for its misfolding

Biochemical and Biophysical Research Communications

Volumn 369, Issue 4, 2008, Pages 1195-1198

  Ikeda, Shino ^a   Kobayashi, Atsushi ^a   Kitamoto, Tetsuyuki ^a  

^a TOHOKU UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

Conversion; N linked glycosylation; Prion protein; Site directed mutagenesis

Indexed keywords

AMINO ACID; ASPARAGINE; PRION PROTEIN; THREONINE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CODON; CONTROLLED STUDY; GLYCOSYLATION; MOUSE; NEUROBLASTOMA CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; SCRAPIE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; ANIMALS; ASPARAGINE; CELL LINE; GLYCOSYLATION; MICE; MUTATION; PRIONS; PROTEIN FOLDING; THREONINE;

EID: 41149163562     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.03.014     Document Type: Article

References (19)

1. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA 95 (1998) 13363-13383
2. van Rheede T., Smolenaars M.M., Madsen O., and de Jong W.W. Molecular evolution of the mammalian prion protein. Mol. Biol. Evol. 20 (2003) 111-121
3. c glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains. J. Neuropathol. Exp. Neurol. 58 (1999) 1000-1009
4. Somerville R.A. Host and transmissible spongiform encephalopathy agent strain control glycosylation of PrP. J. Gen. Virol. 80 (1999) 1865-1872
5. Parchi P., Capellari S., Chen S.G., Petersen R.B., Gambetti P., Kopp N., Brown P., Kitamoto T., Tateishi J., Giese A., and Kretzschmar H. Typing prion isoforms. Nature 386 (1997) 232-234
6. Parchi P., Giese A., Capellari S., Brown P., Schulz-Schaeffer W., Windl O., Zerr I., Budka H., Kopp N., Piccardo P., Poser S., Rojiani A., Streichemberger N., Julien J., Vital C., Ghetti B., Gambetti P., and Kretzschmar H. Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann. Neurol. 46 (1999) 224-233
7. Nitrini R., Rosemberg S., Passos-Bueno M.R., da Silva L.S., Iughetti P., Papadopoulos M., Carrilho P.M., Caramelli P., Albrecht S., Zatz M., and LeBlanc A. Familial spongiform encephalopathy associated with a novel prion protein gene mutation. Ann. Neurol. 42 (1997) 138-146
8. Grasbon-Frodl E., Lorenz H., Mann U., Nitsch R.M., Windl O., and Kretzschmar H.A. Loss of glycosylation associated with the T183A mutation in human prion disease. Acta Neuropathol. 108 (2004) 476-484
9. Neuendorf E., Weber A., Saalmueller A., Schatzl H., Reifenberg K., Pfaff E., and Groschup M.H. Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections. J. Biol. Chem. 279 (2004) 53306-53316
10. Wiseman F., Cancellotti E., and Manson J. Glycosylation and misfolding of PrP. Biochem. Soc. Trans. 33 (2005) 1094-1095
11. Taraboulos A., Rogers M., Borchelt D.R., McKinley M.P., Scott M., Serban D., and Prusiner S.B. Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation. Proc. Natl. Acad. Sci. USA 87 (1990) 8262-8266
12. Sc formation in neuroblastoma cells infected with different prion strains. J. Gen. Virol. 81 (2000) 2555-2563
13. Butler D.A., Scott M.R., Bockman J.M., Borchelt D.R., Taraboulos A., Hsiao K.K., Kingsbury D.T., and Prusiner S.B. Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J. Virol. 62 (1988) 1558-1564
14. Kascsak R.J., Rubenstein R., Merz P.A., Tonna-DeMasi M., Fersko R., Carp R.I., Wisniewski H.M., and Diringer H. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61 (1987) 3688-3693
15. Scott M.R., Kohler R., Foster D., and Prusiner S.B. Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci. 1 (1992) 986-997
16. Asano M., Mohri S., Ironside J.W., Ito M., Tamaoki N., and Kitamoto T. vCJD prion acquires altered virulence through trans-species infection. Biochem. Biophys. Res. Commun. 342 (2006) 293-299
17. DeArmond S.J., Sánchez H., Yehiely F., Qiu Y., Ninchak-Casey A., Daggett V., Camerino A.P., Cayetano J., Rogers M., Groth D., Torchia M., Tremblay P., Scott M.R., Cohen F.E., and Prusiner S.B. Selective neuronal targeting in prion disease. Neuron 19 (1997) 1337-1348
18. Stimson E., Hope J., Chong A., and Burlingame A.L. Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions. Biochemistry 38 (1999) 4885-4895
19. Sun Y., Breydo L., Makarava N., Yang Q., Bocharova O.V., and Baskakov I.V. Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure. J. Biol. Chem. 282 (2007) 9090-9097