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Glycobiology Advance Access published online on April 22, 2009
Glycobiology, doi:10.1093/glycob/cwp062
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Glycosylation-related gene expression profiling in brain and spleen of scrapie-affected mouse

Florence Guillerme-Bosselut1, Lionel Forestier1, Chantal Jayat-Vignoles2, Jean-Luc Vilotte3, Iuliana Popa4,5, Jacques Portoukalian4, Annick Le Dur6, Hubert Laude6, Raymond Julien1 and Paul-François Gallet1,*

1 INRA, UMR1061 Génétique Moléculaire Animale – Université de Limoges, F-87060 Limoges, France
2 CNRS, UMR 6101 Physiologie Moléculaire de la Réponse Immune et des Lymphoproliférations – Université de Limoges, F-87025 Limoges, France
3 INRA, UR1313 Génétique Animale et Biologie Intégrative, F-78350 Jouy-en-Josas, France
4 EA 4169 Université Lyon-1, Hopital Edouard Herriot, F-69000 Lyon, France
5 Institute of Macromolecular Chemistry, Iasi, Romania
6 INRA, UR892 Virologie Immunologie Moléculaires, F-78350 Jouy-en-Josas, France

* Corresponding author: Mailing address: INRA, UMR1061 Génétique Moléculaire Animale – Université de Limoges, Faculté des Sciences et Techniques, 123 Avenue Albert Thomas, 87060 Limoges Cedex. Phone: 335 5545 7654. Fax: 335 5545 7653. E-mail: francois.gallet{at}unilim.fr

Received on December 18, 2008; accepted on April 18, 2009

A central event in the formation of infectious prions is the conformational change of a host-encoded glycoprotein, PrPC, into a pathogenic isoform, PrPSc. The molecular requirements for efficient PrP conversion remain unknown. Altered glycosylation has been linked to various pathologies and the N-glycans harboured by the two prion protein isoforms are different. In order to search for glycosylation-related genes that could mark prion infection, we used a glycosylation dedicated micro-array that allowed the simultaneous analysis of the expression of 165 glycosylation-related genes encoding proteins of the glycosyltransferase, glycosidase, lectin and sulfotransferase families to compare the gene expression profiles of normal and scrapie-infected mouse brain and spleen. Eight genes were found up-regulated in "scrapie brain" at the final state of the disease. In the spleen, 5 genes presented a modified expression. Three genes were also up-regulated in the spleen of infected mice, and two (Pigq and St3gal5) down-regulated. All changes were confirmed by qPCR and biochemical analyses applied to Pigq and St3gal5 proteins.

Key words: brain / gene expression / glycosylation / micro-array / prion disease / spleen


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