Weitergeleitet
durch das Dugi-News-Team am Sonntag, den 22. Juni
2008.
http://www.blackwell-synergy.com/doi/pdf/10.1046/j.1365-2672.2001.01421.x?cookieSet=1
Journal
of
Applied Microbiology 2001, 91, 191±205
A REVIEW
Developments
in microbiological risk
assessment for drinking water
P. Gale
WRc-NSF Ltd,
Medmenham, Marlow,
Buckinghamshire, UK
793/02/01:
received 21 February 2001, revised 6 April 2001 and accepted 27 April
2001
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http://www.arthurmag.com/magpie/?p=2170
Persistent
Prions:
Soilbound Agents are More Potent!
Science News, July 21, 2007; Vol. 172, No. 3 , p. 36
Carolyn
Barry
Deformed
proteins called prions cause fatal
brain-destroying disorders, such as chronic wasting disease in deer and
elk and
mad cow disease, which can infect people. Evidence suggests that prions
make
their way into animals’ nervous systems through ingestion, but
scientists
aren’t sure.
A
new study shows that prions become more
infectious when they latch on to soil particles that animals eat,
suggesting
that ingestion is a primary route of disease transmission. “Our study
points us
in one direction that explains how these animals are getting
infected,†says
study author Judd Aiken of the University of Wisconsin–Madison.
Prions
enter the environment from the remains
of infected animals, and, to some degree, from body fluids such as
urine and
saliva. Prions linger in soil for at least 3 years (see related SN
article
below) by binding tightly to clay and other minerals. Aiken had
hypothesized
that soil would hinder the action of the clingy prions, making them
less
infectious. He was surprised to find the opposite.
“The
binding of infectious agents in soil
actually greatly enhances the infection,†Aiken says. “It makes the
disease
more transmissible.â€
Wild
and farm animals often
swallow up to several hundred grams of soil per day when eating plants,
drinking
muddied water, and licking the ground to get minerals. In
doing so,
they may consume prions. The relationship between ingestion and
infectivity is
unclear, though, because previous experiments showed that prions are
inefficient at infecting animals that eat diseased tissue.
Aiken
and his team fed each of three groups
of hamsters a different soil type containing prions. Other hamsters
were given
an equivalent dose of a prion mixture derived from the brains of
infected
animals. All soil-eating hamsters were at least as likely to contract
the prion
disease as those that had ingested the prion-brain mixture, which has
been
considered an efficient transmitter of prions.
Two
of the three soils had an even more
dramatic effect. Hamsters that ate either of those soils had a higher
rate of
prion disease than did animals that ate the prion-brain mix. Animals
that ate
the third soil, which contained more organic matter than the other two
did, had
the same infection rate as hamsters that ate the prion-brain mix.
Researchers
hypothesize that soil might
protect prions from the destructive environment of the digestive
system.
Alternatively, Aiken says, soil particles might break up clumps of
prions into
smaller, more numerous clusters. Or, the particles could change the way
in which
prions enter nervous system tissues.
The
study, in the July PLoS Pathogens,
yielded “very fascinating findings,†says Michael Miller, a
wildlife
veterinarian at the Colorado Division of Wildlife in Fort Collins.
“It ties
together observations that people have made throughout the years.†He
suggests
that the different infectivity rates of prions in the three soils may
also
explain why the disease afflicts animals in some areas more than in
others.
Prions’
Dirty Little
Secret
Science News, Feb. 11, 2006; Vol. 169, No. 6 , p. 93
Janet
Raloff
Fifteen
years ago, scientists at the National
Institutes of Health reported that malformed prions—proteins that can
trigger
lethal illnesses including mad cow disease—remain on soil surfaces
for at least
3 years. Now, scientists report why rain doesn’t flush away the
prions: The
proteins bind almost irreversibly to clay.
In
fact, clay can “retain up to its own mass
of … prion proteins,†says Peggy Rigou of the National Institute of
Agronomic
Research (INRA) in Jouy-en-Josas, France.
Her
team added sheep prions to pure clay,
sandy soil, and loam. Positively charged parts of the protein molecules
bound
to the negatively charged surface of the clay that was present in all
the soil
samples. Extensive washing failed to dislodge the prions. However, when
the
chemists treated the mixtures to make the proteins negatively charged
and then
ran an electric current through each mixture, the prions migrated off
the clay
particles.
Freeing
the prions was a major achievement,
Rigou notes, because it enables scientists for the first time to
measure prion
concentrations in soil. Until now, no technique could confirm that
intact
prions were present in soil. In an upcoming Environmental Science &
Technology, her team reports that the new procedure permits detection
of
concentrations as low as 0.2 part per billion.
Soils
might acquire prions from animal wastes
or carcasses. Scientists’
concern is that livestock might ingest infected clay
particles while eating grass or drinking from mud puddles,
Rigou says.
PRION
is
an acronym
for a unique infectious agent called a prion (proteinaceous infectious
particle), composed of abnormal proteinaceous material devoid of
detectable
amounts of nucleic acid. These are abnormal versions of prion protein,
or “PrPâ€
which is ubiquitous to cell membranes, but is highly species specific.
These
infective agents can infect cows in the form of Bovine Spongiform
Encephalopathy (BSE) and is also known as “Mad Cows Disease†.
Feline Spongiform
Encephalopathy (FSE) occurs in cats. In sheep and goats, the disease is
called
Scrapie, In mink, the disease is Transmissible Mink encephalopathy
(TME). In
mule deer and elk, the disease is called Chronic Wasting disease. Human
disease
can be classified as Creutzfeldt-Jakob Disease (CJD), variant CJD
(vCJD),
Gerstmann-Staussler-Scheinker Disease (GSS), Kuru, Fatal Familial
Insomnia
(FFI), or in infants, Alpers Syndrome.
Virulence
Factors: Prions are proteins. The
body encodes a gene for a normal protein, PrP, usually found in
lymphocytes and
CNS neurons. PrP has a normal conformation known as PrPc, which is
genetically
encoded. It becomes misfolded into a form known as PrPsc, and causes
other
proteins to become misfolded as well.
The
protein goes from a 40% alpha helix with
almost no beta sheet to 30% alpha helix and 45% beta sheet but retains
same
amino acid sequence. It had previously been thought that the amino acid
sequence could have mainly one active structure, but this shows
that’s not
true. Unlike PrPc, the misfolded PrPsc is not easily digested by
proteases. It
does not cause an immune response. The abnormal protein can’t be
broken down in
the body and so it aggregates in the brain.
These
particles do not infect cells or
tissues and propagate, but rather are able to convert normal prion
proteins
into the abnormal form. The
conversion rate is logarithmic but slow.
![]()
Wilfried
Soddemann
Ltd.
Regierungsbaudirektor a.D.
Bauassessor
Dipl.-Ing.
![]()
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Das
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Giftcocktail von Spurenschadstoffen und Bakterien, Parasiten, Viren und
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