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From: TSS ()
Subject: Rare Brain Disease Could Be to Blame for Three Northeast Indiana Deaths
Date: May 19, 2007 at 7:14 am PST

A NewsChannel 15 Exclusive
Rare Brain Disease Could Be to Blame for Three Northeast Indiana Deaths

May 17, 2007 11:03 PM CDT

(Fort Wayne - WANE) Newschannel 15 has learned that three people in
northeast Indiana may have died in the last six months from an extremely
rare brain disease. The Centers for Disease Control estimates your chance of
getting it at one in a million.

The disease is similar to mad cow disease, a condition where the proteins in
an animal's brain stop working normally and start to eat holes in the living

The same thing can happen in humans afflicted with Creutzfeldt-Jakob
disease. The Fort Wayne - Allen County Health Department has confirmed three
reported fatal cases of Creutzfeldt-Jakob disease or CJD over the past six

Most of the time, people randomly develop the disorder. Doctors don't know
why it happens. While it is very rare, people can get CJD by eating beef
contaminated with mad cow disease. That happened in the United Kingdom, but
has not happened in the United States.

Indiana doesn't consider Creutzfeldt-Jakob disease a reportable illness,
which means cases aren't tracked, documented or investigated in the state.
Local health officials are working to make CJD a reportable disease, that
way they can learn more about it.

Fort Wayne - Allen County Health Department Commissioner Deborah McMahan, MD
says seeing three cases in six months has gotten her attention. But she
doesn't think people should worry about the food supply being contaminated.

Kinds of Creutzfeldt-Jakob Disease:

There are three kinds of Creutzfeldt-Jakob disease, or CJD. Most cases,
about 85%, are known as sporadic CJD. For some reason, and doctors don't
know why, proteins called prions mutate. The abnormal prion then affects
other proteins around it, causing them to lose their ability to function.
The brain starts turning spongy and holes are eaten out of it.

Around 5-15% of CJD cases are classified as familial CJD. This is when a
person inherits the abnormal protein (prion). A person with familial CJD has
a 50/50 chance of passing the gene mutation to his or her children.

The third kind of CJD is known as a new variant CJD or vCJD, and accounts
for less than 1% of CJD cases. This type is not related to classic sporadic
or familial CJD. vCJD happens when a person gets infected with the mutated
protein from an outside source.

One of the most well-known ways is from eating food contaminated with mad
cow disease. This was first detected in 1996 in the United Kingdom.

vCJD cases have also occurred when people had surgery and surgical
instruments were contaminated. Now sterilization procedures prevent that
from happening.

A third way vCJD was contracted was through a growth hormone made from the
pituitary glands of cadavers. The mutated prion can't be killed with
traditional disinfection procedures, so they were carried into the hormone
pills. Now the hormone supplements are made artificially, so there is no
chance of contamination.

Symptoms of Creutzfeldt-Jakob Disease:

There are many symptoms associated with CJD and they can vary in different
people. Symptoms include:

* Personality changes

* Muscle twitching or stiffness

* Hallucinations

* Nervousness, jumpy feelings

* Stumbling or falling

* Speech impairment or enunciation problems

* Memory loss

* Anxiety, stress and tension

Diagnosis and Treatment of Creutzfeldt-Jakob Disease:

Several tests can recognize signs of CJD, but only an autopsy can confirm
it. An electroencephalograph (EEG) measures electrical brain activity. It
can detect changes in the brain if other symptoms have been present for
three months.

A spinal tap can detect abnormal proteins in the spinal fluid. Along with
other symptoms, that can lead doctors to believe someone has CJD.

There is no way to prevent sporadic or familial CJD, and there is no
treatment for it. People can treat the symptoms, but most only live for
about six months after being diagnosed.

Sources: National Library of Medicine, National Institutes of Health,

Conversion of the BASE Prion Strain
into the BSE Strain: The Origin of BSE?

Raffaella Capobianco1, Cristina Casalone2, Silvia Suardi1, Michela
Mangieri1, Claudia Miccolo1, Lucia Limido1,
Marcella Catania1, Giacomina Rossi1, Giuseppe Di Fede1, Giorgio Giaccone1,
Maria Grazia Bruzzone1, Ludovico Minati1,
Cristiano Corona2, Pierluigi Acutis2, Daniela Gelmetti3, Guerino Lombardi3,
Martin H. Groschup4, Anne Buschmann4,
Gianluigi Zanusso5, Salvatore Monaco5, Maria Caramelli2, Fabrizio
1 Fondazione I.R.C.C.S. Istituto Neurologico Carlo Besta, Milan, Italy, 2
Istituto Zooprofilattico Sperimentale del Piemonte, Liguria e Valle d’Aosta,
Torino, Italy, 3 Istituto
Zooprofilattico Sperimentale della Lombardia ed Emilia Romagna, Brescia,
Italy, 4 Friedrich-Loeffler-Institut, Institute for Novel and Emerging
Infectious Diseases, Greifswald,
Insel Riems, Germany, 5 Department of Neurological and Visual Science,
Section of Clinical Neurology, Policlinico G. B. Rossi, Verona, Italy

Atypical neuropathological and molecular phenotypes of bovine spongiform
encephalopathy (BSE) have recently been
identified in different countries. One of these phenotypes, named bovine
‘‘amyloidotic’’ spongiform encephalopathy
(BASE), differs from classical BSE for the occurrence of a distinct type of
the disease-associated prion protein (PrP),
termed PrPSc, and the presence of PrP amyloid plaques. Here, we show that
the agents responsible for BSE and BASE
possess different biological properties upon transmission to transgenic mice
expressing bovine PrP and inbred lines of
nontransgenic mice. Strikingly, serial passages of the BASE strain to
nontransgenic mice induced a neuropathological
and molecular disease phenotype indistinguishable from that of BSE-infected
mice. The existence of more than one
agent associated with prion disease in cattle and the ability of the BASE
strain to convert into the BSE strain may have
important implications with respect to the origin of BSE and spongiform
encephalopathies in other species, including

Citation: Capobianco R, Casalone C, Suardi S, Mangieri M, Miccolo C, et al.
(2007) Conversion of the BASE prion strain into the BSE strain: The origin
of BSE? PLoS Pathog 3(3):
e31. doi:10.1371/journal.ppat.0030031



Although BASE showed a significant barrier to primary
transmission to inbred mouse lines resulting in preclinical
infection, it remains of considerable concern whether the
causal agent is potentially pathogenic for humans. In this
regard, the neuropathological and molecular features of
BASE—in particular, the biochemical type and deposition
patterns of PrPSc—have striking similarities with those of a
distinct subgroup of patients with sporadic CJD [16]. This
finding requires a cautious interpretation. Nonetheless, the
possibility that the origin of CJD in some patients with a
sporadic disease phenotype may be related to BASE exposure
has to be considered and verified through transmission studies.

see full text ;


18 January 2007 - Draft minutes of the SEAC 95 meeting (426 KB) held on 7
December 2006 are now available.


64. A member noted that at the recent Neuroprion meeting, a study was
presented showing that in transgenic mice BSE passaged in sheep may be more
virulent and infectious to a wider range of species than bovine derived BSE.

Other work presented suggested that BSE and bovine amyloidotic spongiform
encephalopathy (BASE) MAY BE RELATED. A mutation had been identified in the


3:30 Transmission of the Italian Atypical BSE (BASE) in Humanized Mouse

Models Qingzhong Kong, Ph.D., Assistant Professor, Pathology, Case Western

Bovine Amyloid Spongiform Encephalopathy (BASE) is an atypical BSE strain
discovered recently in Italy, and similar or different atypical BSE cases
were also reported in other countries. The infectivity and phenotypes of
these atypical BSE strains in humans are unknown. In collaboration with
Pierluigi Gambetti, as well as Maria Caramelli and her co-workers, we have
inoculated transgenic mice expressing human prion protein with brain
homogenates from BASE or BSE infected cattle. Our data shows that about half
of the BASE-inoculated mice became infected with an average incubation time
of about 19 months; in contrast, none of the BSE-inoculated mice appear to
be infected after more than 2 years.

***These results indicate that BASE is transmissible to humans and suggest
that BASE is more virulent than
classical BSE in humans.***

6:30 Close of Day One

1997 TO 2006. SPORADIC CJD CASES TRIPLED, with phenotype
of 'UNKNOWN' strain growing. ...

There is a growing number of human CJD cases, and they were presented last
week in San Francisco by Luigi Gambatti(?) from his CJD surveillance

He estimates that it may be up to 14 or 15 persons which display selectively
SPRPSC and practically no detected RPRPSC proteins.

Diagnosis and Reporting of Creutzfeldt-Jakob Disease

Singeltary, Sr et al. JAMA.2001; 285: 733-734.





MARCH 26, 2003

RE-Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob

disease in the United States

Email Terry S. Singeltary:

I lost my mother to hvCJD (Heidenhain Variant CJD). I would like to

comment on the CDC's attempts to monitor the occurrence of emerging

forms of CJD. Asante, Collinge et al [1] have reported that BSE

transmission to the 129-methionine genotype can lead to an alternate

phenotype that is indistinguishable from type 2 PrPSc, the commonest

sporadic CJD. However, CJD and all human TSEs are not reportable

nationally. CJD and all human TSEs must be made reportable in every

state and internationally. I hope that the CDC does not continue to

expect us to still believe that the 85%+ of all CJD cases which are

sporadic are all spontaneous, without route/source. We have many TSEs in

the USA in both animal and man. CWD in deer/elk is spreading rapidly and

CWD does transmit to mink, ferret, cattle, and squirrel monkey by

intracerebral inoculation. With the known incubation periods in other

TSEs, oral transmission studies of CWD may take much longer. Every

victim/family of CJD/TSEs should be asked about route and source of this

agent. To prolong this will only spread the agent and needlessly expose

others. In light of the findings of Asante and Collinge et al, there

should be drastic measures to safeguard the medical and surgical arena

from sporadic CJDs and all human TSEs. I only ponder how many sporadic

CJDs in the USA are type 2 PrPSc?

Terry S. Singeltary Sr.
P.O. Box 42
Bacliff, Texas USA 77518

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