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From: TSS ()
Subject: Both host prion protein 131–188 subregion and prion strain characteristics regulate glycoform of PrPSc
Date: March 9, 2007 at 9:10 am PST

Both host prion protein 131–188 subregion and prion strain characteristics regulate glycoform of PrPSc
Journal Archives of Virology
Publisher Springer Wien
ISSN 0304-8608 (Print) 1432-8798 (Online)
Subject Biomedical and Life Sciences and Medicine
Issue Volume 152, Number 3 / March, 2007
DOI 10.1007/s00705-006-0858-0
Pages 603-609
SpringerLink Date Wednesday, November 15, 2006


T. Yokoyama1, K. Shimada1, K. Masujin1, Y. Iwamaru1, M. Imamura1, Y. K. Ushiki1, 2, K. M. Kimura1, S. Itohara3 and M. Shinagawa1

(1) Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki, Japan
(2) Nippi Research Institute of Biomatrix, Toride, Ibaraki, Japan
(3) Brain Science Institute, RIKEN, Wako, Saitama, Japan

Received: 5 March 2006 Accepted: 16 August 2006 Published online: 16 November 2006

Summary. Prion proteins (PrPs) contain 2 N-linked glycosylation sites and are present in cells in 3 different forms. An abnormal isoform of prion protein (PrPSc) has different glycoform patterns for different prion strains. However, the molecular basis of the strain-specific glycoform variability in prions has remained elusive. To understand the molecular basis of these glycoform differences, we analyzed PrPSc in 2 lines of transgenic mice (MHM2 and MH2M with PrP null background) that expressed a chimeric PrP. Our result indicated that PrP 131–188 (substitutions at I139M, Y155N, and S170N) contributed to both PrPC and PrPSc glycoform ratios. Furthermore, the PrPSc glycoform pattern within these transgenic mice showed a subtle difference depending on the inoculated prion. This study indicated that the PrPSc glycoform ratio was influenced by both host PrPC and the prion strain.

http://www.springerlink.com/content/k72168ukn747k754/


TSS




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