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From: TSS ()
Subject: High Titers of Transmissible Spongiform Encephalopathy Infectivity Associated with Extremely Low Levels of PrPSc in Vivo*
Date: November 30, 2007 at 9:56 am PST

J. Biol. Chem., Vol. 282, Issue 49, 35878-35886, December 7, 2007


High Titers of Transmissible Spongiform Encephalopathy Infectivity
Associated with Extremely Low Levels of PrPSc in Vivo*

Rona M. Barron12, Susan L. Campbell13, Declan King, Anne Bellon, Karen E.
Chapman¶, R. Anthony Williamson, and Jean C. Manson
From the Neuropathogenesis Unit, Roslin Institute, Ogston Building, West
Mains Road, Edinburgh EH9 3JF, Scotland, United Kingdom, the Department of
Immunology, Scripps Research Institute, La Jolla, California 92037, and the
¶Centre for Cardiovascular Sciences, Queen's Medical Research Institute,
University of Edinburgh, 47 Little France Crescent, Edinburgh EH16 4TJ,
Scotland, United Kingdom

Diagnosis of transmissible spongiform encephalopathy (TSE) disease in humans
and ruminants relies on the detection in post-mortem brain tissue of the
protease-resistant form of the host glycoprotein PrP. The presence of this
abnormal isoform (PrPSc) in tissues is taken as indicative of the presence
of TSE infectivity. Here we demonstrate conclusively that high titers of TSE
infectivity can be present in brain tissue of animals that show clinical and
vacuolar signs of TSE disease but contain low or undetectable levels of
PrPSc. This work questions the correlation between PrPSc level and the titer
of infectivity and shows that tissues containing little or no proteinase
K-resistant PrP can be infectious and harbor high titers of TSE infectivity.
Reliance on protease-resistant PrPSc as a sole measure of infectivity may
therefore in some instances significantly underestimate biological
properties of diagnostic samples, thereby undermining efforts to contain and
eradicate TSEs.

---------------------------------------------


Received for publication, May 25, 2007 , and in revised form, September 24,
2007.

* This work was supported by United Kingdom Department for Environment,
Food, and Rural Affairs Grant SE1437. The costs of publication of this
article were defrayed in part by the payment of page charges. This article
must therefore be hereby marked "advertisement" in accordance with 18 U.S.C.
Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org)
contains supplemental Figs. S1–S3 and Table S1.

1 Both authors contributed equally to this work.

3 Current address: Medical Research Council Clinical Sciences Centre,
Imperial College, Hammersmith Campus, Du Cane Road, London W12 0NN, United
Kingdom.

2 To whom correspondence should be addressed. Tel.: 44-131-667-5204; Fax:
44-131-668-3872; E-mail: rona.barron@bbsrc.ac.uk.


http://www.jbc.org/cgi/content/abstract/282/49/35878?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&fulltext=prion&searchid=1&FIRSTINDEX=0&volume=282&issue=49&resourcetype=HWCIT


TSS




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