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Veterinary Microbiology 123 (2007) 285–286

Preface

Prion research: Past, present, and future

Transmissible spongiform encephalopathies (TSEs)

are unique diseases in terms of their pathophysiology,

pathogenesis and agent characteristics that affect

animals and humans. In man, sporadic, genetic and

acquired forms are known. A characteristic feature of

all TSEs, including hereditary and sporadic forms, is the

replication of an unconventional agent in the brain,

which can transmit the disease within and across

different species. This process is accompanied by the

deposition of an aberrant form of the host-derived

prion protein (PrP) with a pathologically altered folding

and/or aggregation structure. The prion hypothesis

holds that the causative agents of TSEs provide a

new biological principle of infection: Proteinaceous

infectious particles (‘‘prions’’) which are essentially

composed of misfolded prion protein, known as

PrPSc.

For decades, the enigmatic aetiology of TSEs and

the puzzling biochemical and biophysical properties

of their transmissible agent have fuelled a vivid and

controversial debate in the scientific community. As a

result of the bovine spongiform encephalopathy (BSE)

epidemic and its subsequent zoonotic transmission to

humans which has so far led to 201 reported cases of

variant Creutzfeldt-Jakob disease (vCJD) worldwide,

the potential risks posed by TSEs became clearly

visible. These risks are a major challenge for veterinary

and human medicine as well as for agricultural and

public health policies.

A number of individual countries as well as the

European Union have therefore invested enormous

time and energy into addressing BSE and vCJD

problems as well as the issues raised by scrapie, the

archetype of all TSEs in sheep and goats. This has

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doi:10.1016/j.vetmic.2007.03.031

included furtherance of research into TSEs, since it is

believed that a better scientific understanding of these

diseases and their pathogens will provide the best basis

for their containment, prevention and eradication.

In Germany, the government sponsored the foundation

of a National TSE Research Platform in which

scientists from different disciplines successfully

worked together on research projects relating to the

aetiology, pathogenesis, diagnosis, prevention, ther-

apy and epidemiology of TSEs. This special issue of

veterinary microbiology is an anthology of some of

the achievements reported at the final meeting of the

German TSE Research Platform held from 26 June to

28 June 2006 in Greifswald.

The support given to TSE networks and — projects

has succeeded in rendering more cohesive previously

fragmented research as well as in stimulating the

scientific output in terms of both quality and quantity.

Sustained scientific knowledge and excellence are

absolutely key to being well-prepared to deal with the

different and varied eventualities and changes that

may occur in the development of TSEs, such as the

recent emergence of atypical scrapie and atypical

BSE, or the alarming spread of chronic wasting

disease in North America. Potentially even more

important, the replication of misfolded prion proteins

may result, in principle, in a paradigm for a broader

spectrum of proteinopathies (i.e. protein folding and

aggregation disorders). Therefore, investment in TSE

research goes beyond supporting work on scrapie,

BSE or Creutzfeldt-Jakob disease in their own

right—it may well also contribute to a better under-

standing of the key molecular mechanisms involved in

Alzheimer’s disease and other amyloidoses. Inducible

.

Preface / Veterinary Microbiology 123 (2007) 285–286286

proteinopathies such as amyloid A amyloidosis or

apolipoprotein A II amyloidosis show remarkable

similarities to prion diseases (Walker et al., 2006), and

most recently Meyer-Luehmann et al. (2006) reported

that in the context of Alzheimer’s disease the

exogenous induction of cerebral b-amyloidogenesis

is governed by agent and host. Such striking parallels

to infectious prion diseases are calling out for a clearer

delimitation and possibly even a new molecular

definition of diseases resulting from pathological

protein misfolding and assembly.

References

Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser,

S., Schaefer, C., Kilger, E., Neuenschwander, A., Abra-

mowski, D., Frey, P., Jaton, A.L., Vigouret, J.M., Paganetti,

P., Walsh, D.M., Mathews, P.M., Ghiso, J., Staufenbiel, M.,

Walker, L.C., Jucker, M., 2006. Exogenous induction of

cerebral beta-amyloidogenesis is governed by agent and host.

Science 313, 1781–1784.

Walker, L.C., Levine III, H., Mattson, M.P., Jucker, M., 2006.

Inducible proteopathies. Trends Neurosci. 29, 438– 443.

Michael Beekes*

P24, Transmissible Spongiform Encephalopathies,

Robert-Koch-Institute Nordufer 20, 13353 Berlin,

Germany

Inga Zerr1

National TSE Reference Centre, Department of

Neurology, Georg-August University, Gottingen,

Germany

Martin H. Groschup2

Institute for Novel and Emerging Infectious Diseases

at the Friedrich-Loeffler-Institut, Boddenblick 5a,

17493 Greifswald, Germany

*Corresponding author.

Tel.: +49 30 4547 2396; fax: +49 30 4547 22671Tel.: +49 551 396636; fax: +49 551 397020.

2Tel.: +49 38351 7 163; fax: +49 38351 7 191.

E-mail address: IngaZerr@med.uni-goettingen.de

(I. Zerr)

BeekesM@rki.de (M. Beekes)

martin.groschup@fli.bund.de (Martin H. Groschup)