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Neurosci Lett. 2006 Nov 20;408(3):165-9. Epub 2006 Oct 9.

V180I mutation of the prion protein gene associated with atypical PrPSc glycosylation.

Author information

1
UPRES EA 3621, UFR des Sciences Pharmaceutiques et Biologiques, Université Paris 5 et Service de Biochimie et Biologie Moléculaire, Hôpital Lariboisière, 2 rue A. Paré, 75475 Paris cedex 10, France.

Abstract

A valine to isoleucine mutation at residue 180 was identified in a French patient with Creutzfeldt-Jakob disease (CJD). The mutation is located in the close vicinity of one of the two N-glycosylation sites of the cellular prion protein (PrP(C)). Western blot analysis revealed accumulation in the brain of the pathogenic proteinase K-resistant PrP (PrP(Sc)) isoform with the notable absence of the diglycosylated band. The mutant protein expressed in CHO cells was correctly glycosylated, suggesting that the atypical glycosylation pattern of PrP(Sc) was not due to the mutation at position 180. These results suggest that the diglycosylated form of the mutant PrP(180I) prevents its conversion into the pathogenic mutant form PrP(Sc180I), supporting a central role of N-linked glycan chains in the PrP conversion process.

PMID:
17029785
DOI:
10.1016/j.neulet.2006.08.008
[Indexed for MEDLINE]

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