Sialylated and O-glycosidically linked glycans in prion protein deposits in a case of Gerstmann-Sträussler-Scheinker disease.
Prion diseases are caused by an abnormal form of the prion protein (PrP(Sc)). We identified, with lectins, post-translational modifications of brain proteins due to glycosylation in a Gerstmann-Sträussler-Scheinker (GSS) patient. The lectin Amaranthus leucocarpus (ALL), specific for mucin type O-glycosylated structures (Galß1,3 GalNAcα1,0 Ser/Thr or GalNAcα1,0 Ser/Thr), and Sambucus nigra agglutinin (SNA), specific for Neu5Acα2,6 Gal/GalNAc, showed positive labeling in all the prion deposits and in the core of the PrP(Sc) deposits, respectively, indicating specific distribution of O-glycosylated and sialylated structures. Lectins from Maackia amurensis (MAA, Neu5Acα2,3), Macrobrachium rosenbergii (MrL, Neu5,9Ac2-specific) and Arachis hypogaea (PNA, Gal-specific) showed low staining of prion deposits. Immunohistochemistry colocalization with prion antibody indicated that all lectins stained prion protein deposits. These results show that specific modifications in the glycosylation pattern are closely related to the hallmark lesions and might be an early event in neuronal degeneration in GSS disease.
Zomosa-Signoret
Viviana
V
Laboratorio Experimental de Enfermedades Neurodegenerativas, Instituto Nacional de Neurología, Mexico.
Mayoral
Miguel
M
Limón
Daniel
D
Espinosa
Blanca
B
Calvillo
Minerva
M
Zenteno
Edgar
E
Martínez
Victor
V
Guevara
Jorge
J
D016098:Gerstmann-Straussler-Scheinker Disease / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D007150:Immunohistochemistry; D037102:Lectins; D018613:Microscopy, Confocal; D046529:Microscopy, Electron, Transmission; D008875:Middle Aged; D011134:Polysaccharides / Q000378:metabolism*; D018620:PrPSc Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D037102:Lectins; D011134:Polysaccharides; D018620:PrPSc Proteins