Prions: Protein Aggregation and Infectious Diseases - Physiological ...

1140 ADRIANO AGUZZI AND ANNA MARIA CALELLA
on the quality of the tools and technologies available to
the prion field. These unresolved questions provide an
opportunity for additional research which may have a
significant impact on further protein misfolding disorders.
ACKNOWLEDGMENTS
This article honors the present and past members of the
Aguzzi laboratory, whose enthusiastic commitment led to much
of the work described here. Special thanks to Petra Schwarz for
maintaining our prion-infected mouse colony in impeccable
shape and to Rita Moos for excellent technical assistance.
Mathias Heikenwälder, Christina Sigurdson, Jeppe Falsig, and
Mario Nuvolone provided crucial help with the section on “Immunological
aspects of Prion disease” and Simone Hornemann
with the section on “Structures of purified PrP C and PrP Sc .”
Certain parts of the history of prion research were adapted from
a previously published book chapter [A. Aguzzi. In: Topley &
Wilson’s Microbiology and Microbial Infections (10 th ed.), 2005]
whose previous edition had been published by Dr. Stanley B.
Prusiner. We are grateful to Dr. Prusiner for giving us permission
to utilize some of his material.
Address for reprint requests and other correspondence: A.
Aguzzi, Institute of Neuropathology, University Hospital Zürich,
Schmelzbergstrasse 12, CH-8091 Zürich, Switzerland (e-mail:
adriano.aguzzi@usz.ch).
GRANTS
A. Aguzzi is supported by grants from the University of Zurich;
the Swiss Federal Offices of Education, Science, and Health; the
Swiss National Foundation; the National Center for Competence in
Research on neural plasticity and repair; the United Kingdom Department
for Environment, Food, and Rural Affairs; and the
Stammbach Foundation. A. M. Calella was supported by the Roche
Research Foundation and an EMBO fellowship.
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