Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid.

Abstract:

:The only identified component of the scrapie prion is PrPSc, a glycosylinositol phospholipid (GPI)-linked protein that is derived from the cellular isoform (PrPC) by an as yet unknown posttranslational event. Analysis of the PrPSc GPI has revealed six different glycoforms, three of which are unprecedented. Two of the glycoforms contain N-acetylneuraminic acid, which has not been previously reported as a component of any GPI. The largest form of the GPI is proposed to have a glycan core consisting of Man alpha-Man alpha-Man-(NeuAc-Gal-GalNAc-)Man-GlcN-Ino. Identical PrPSc GPI structures were found for two distinct isolates or "strains" of prions which specify different incubation times, neuropathology, and PrPSc distribution in brains of Syrian hamsters. Limited analysis of the PrPC GPI reveals that it also has sialylated glycoforms, arguing that the presence of this monosaccharide does not distinguish PrPC from PrPSc.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Stahl N,Baldwin MA,Hecker R,Pan KM,Burlingame AL,Prusiner SB

doi

10.1021/bi00136a600

subject

Has Abstract

pub_date

1992-06-02 00:00:00

pages

5043-53

issue

21

eissn

0006-2960

issn

1520-4995

journal_volume

31

pub_type

杂志文章