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Is BSE Caused By a VIRUS?

A

Anonymous

Guest
Health/ScienceStudy challenges mad cow research
BLOOMBERG NEWS

January 31, 2007

Researchers have found more evidence that a virus may cause mad cow disease and a related brain disorder in humans, threatening to overturn 25 years of research focusing on malformed proteins called prions.

Nerve cells infected with the human form of mad cow disease contained a virus-sized particle that doesn't appear in uninfected cells, said Laura Manuelidis, a neuropathologist at Yale Medical School in New Haven, Conn. Cells infected with scrapie, a sheep disorder related to mad cow disease, contained the same germ.




The findings raise the possibility of vaccines against the diseases and challenge research showing the disorders are spread by prions, abnormal proteins that have also been detected in the brains of infected humans and animals.

Some scientists have questioned the prion research performed by Stanley Prusiner of the University of California, San Francisco, since he won the Nobel Prize in 1997, Manuelidis said.

"If you don't look for something, you're not going to find it," she said in a telephone interview. "If everyone believes the world is flat, no one will go out and try to find the end."

Mad cow disease, otherwise known as bovine spongiform encephalopathy, is one of a family of rare infections that cause slow, relentless brain damage in humans and animals. The disease often takes years to appear and develop, making research especially time-consuming.

Questions about whether prions cause the infections have arisen because people and animals are thought to catch the diseases by eating tainted meat. The human stomach and intestines would quickly break down any protein, normal or abnormal, before it reached the blood or brain, said Sheldon Penman, an emeritus professor of biology at Massachusetts Institute of Technology.

Proteins, the building blocks of cells and tissues, aren't normally considered carriers of infections, like bacteria and viruses, he said. The Nobel Prize-winning work by the University of California's Prusiner lacked the precision to show that injections of prions transmitted the disease, Penman said.

"He injected stuff that had prions in it, including a million other things," Penman said in an interview. "He never did the crucial experiment of injecting prion protein and inducing disease."

Prusiner won the Nobel in physiology or medicine in 1997 "for his discovery of prions - a new biological principle of infection." He declined an interview through a university spokeswoman.

Scientists have been trying to gain a better understanding of mad cow disease, or BSE, since it struck United Kingdom herds in the late 1980s. About 153 people have developed the human form, called variant Creutzfeldt-Jakob disease, or vCJD, and health officials have put restrictions on animal feeding practices to prevent infections.

Manuelidis published research in 2005 showing that infections with a mild form of vCJD protected mice against more severe infections with the same disease. The findings suggested that vaccines against such human and animal diseases might be possible, she said at the time.

In the study published Monday, she and her colleagues studied colonies of cells with and without the human and sheep infections. They found that only infected cells contained a particle at the smaller end of the range associated with viruses.

The particles were configured in rows and groupings that appear similar to the way viruses sometimes congregate in cells, Manuelidis said. Using immune proteins called antibodies, the Yale team determined that the particles are not made of prion protein. The findings appear online in the Proceedings of the National Academy of Sciences.
 

TimH

Well-known member
Quote-(from the article)

"The human stomach and intestines would quickly break down any protein, normal or abnormal, before it reached the blood or brain, said Sheldon Penman, an emeritus professor of biology at Massachusetts Institute of Technology. "

BLASPHEMY!!! How dare anyone question Dr. Prusiner's Nobel Prize winning work!!!!!
What the hell does a biology professor from MIT know anyway? :wink:

:D :D :D :D :D
 

rkaiser

Well-known member
TimH Posted: Wed Jan 31, 2007 5:43 pm Post subject:

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

Quote-(from the article)

Quote:
"The human stomach and intestines would quickly break down any protein, normal or abnormal, before it reached the blood or brain, said Sheldon Penman, an emeritus professor of biology at Massachusetts Institute of Technology. "


BLASPHEMY!!! How dare anyone question Dr. Prusiner's Nobel Prize winning work!!!!!
What the hell does a biology professor from MIT know anyway?

Careful Oldtimer - if you read the part of the article that Tim presented, and consider it ---- you and your Rclown buds may not have an arguement for a closed border any more. You're balancing on a rather small cherry picker leaf in the BSeconomic pond as it is.
 
A

Anonymous

Guest
Still boils down to the same thing tho Kaiser-- there are still so many unanswered questions about cause and transmission of BSE/TSE's that we should not be weakening any of our firewalls and safeguards...Studies like this raises more questions- and brings many of the previous theories into doubt...
And USDA has said over and over that the number 1 safeguard the US had against BSE was our import rule quarantine on cattle/beef ....
 

rkaiser

Well-known member
Still boils down to the same old thing Oldtimer - that boil on the side of your head that stops you from thinkin about anything else but a closed border - no matter how much it pads Cargill and Tysons pockets.
 

rkaiser

Well-known member
Talkin about thinkin Oldtimer. Here is a little peom that I read on the side of a fellows barn one time.

Sometimes I think I think too much
and sometimes when I do
I try to think what others think
and that gets me in doo doo.
Think for yourself.

That little poem would be good for a lot of folks to take heed to here on ranchers. Oldtimer thinks that all that is right is that which a few Rcalf protectionists think is right.

Scott and Tam --- well we all know what they think.

Cargill and Tyson - on the other hand - well they hire thinkers, thinkers that tell them how to make money and walk the fine line between legal and illegal. Thinkers who think about ways to keep puppets like Tam and Scott fighting their battles for them.

Be nice if there were a few more free thinkers on this site. Get's a little boring coming back here and seeing the same posts month after month.
 

flounder

Well-known member
rkaiser said:
TimH Posted: Wed Jan 31, 2007 5:43 pm Post subject:

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

Quote-(from the article)

Quote:
"The human stomach and intestines would quickly break down any protein, normal or abnormal, before it reached the blood or brain, said Sheldon Penman, an emeritus professor of biology at Massachusetts Institute of Technology. "


BLASPHEMY!!! How dare anyone question Dr. Prusiner's Nobel Prize winning work!!!!!
What the hell does a biology professor from MIT know anyway?

Careful Oldtimer - if you read the part of the article that Tim presented, and consider it ---- you and your Rclown buds may not have an arguement for a closed border any more. You're balancing on a rather small cherry picker leaf in the BSeconomic pond as it is.


dang rkeiser, if you are refering to the fact the TSE ''agent'' as i have always said, which can survive ashing to 600 degrees C., and the fact that it would not matter if it was a prion or a virus or something in between, it's still one mean mother, if you are refering to that, i must give you more credit than you deserve :wink:


TSS



Subject: Cells infected with scrapie and Creutzfeldt–Jakob disease agents produce intracellular 25-nm virus-like particles
Date: January 31, 2007 at 10:28 am PST
Cells infected with scrapie and Creutzfeldt–Jakob

disease agents produce intracellular 25-nm

virus-like particles


Laura Manuelidis*, Zhoa-Xue Yu, Nuria Banquero, and Brian Mullins

Yale Medical School, 333 Cedar Street, New Haven, CT 06510

Communicated by Sheldon Penman, Massachusetts Institute of Technology, Cambridge, MA, December 11, 2006 (received for review October 10, 2006)

We had repeatedly found 25-nm-diameter virus-like particles in

highly infectious brain fractions with little prion protein (PrP), and

therefore we searched for similar virus-like particles in situ in

infected cell lines with high titers. Neuroblastoma cells infected

with the 22L strain of scrapie as well as hypothalamic GT cells

infected with the FU Creutzfeldt–Jakob disease agent, but not

parallel mock controls, displayed dense 25-nm virus-like particles in

orthogonal arrays. These particles had no relation to abnormal PrP

amyloid in situ, nor were they labeled by PrP antibodies that

faithfully recognized rough endoplasmic reticulum membranes

and amyloid fibrils, the predicted sites of normal and pathological

intracellular PrP. Additionally, phorbol ester stimulated the production

of abnormal PrP gel bands by>5-fold in infected N2a22L

cells, yet this did not increase either the number of virus-like arrays

or the infectious titer of these cells. Thus, the 25-nm infectionassociated

particles could not be prions. Synaptic differentiation

and neurodegeneration, as well as retroviruses that populate the

rough endoplasmic reticulum of neuroblastoma cells, were not

required for particle production. The 25-nm particle arrays in

cultured cells strongly resembled those first described in 1968 in

synaptic regions of scrapie-infected brain and subsequently identified

in many natural and experimental TSEs. The high infectivity

of comparable, isolated virus-like particles that show no intrinsic

PrP by antibody labeling, combined with their loss of infectivity

when nucleic acid–protein complexes are disrupted, make it likely

that these 25-nm particles are the causal TSE virions that induce

late-stage PrP brain pathology.



snip.



In summation, all of this data provides a clear, consistent,

substantive, and logical alternative to the accepted prion hypothesis.

The causative TSE agent is most consistent with an

exogenous 25-nm virion without intrinsic host PrP. The stimulation

of host innate immune responses by these agents, a

complex set of molecular reactions that precedes the elaboration

of pathologic PrP (9) and one that is not provoked by PrP-res

itself (25), also point to a foreign pathogen rather than some

unpredictably spontaneous mutation in the host’s PrP without

cause. The presence of these particles in many different species

infected with a wide variety of TSE strains is in accord with

Koch’s first requirement (1). It is also improbable that an

identical virus-like structure would be a contaminant or a

secondary coincidental feature of all these different TSE models.

Nevertheless, a more detailed molecular analysis of these

particles will be required to substantiate their causal nature.

Purification of these 25-nm particles from productive tissue

cultures should be informative if the essential infectivity assays

are performed systematically with parallel ultrastructural and

molecular analyses. Animal titrations of infectivity are expensive

and prolonged. However, sustained and reproducible infection

of indicator GT cells by a variety of TSE agents already has

shown that they can rapidly authenticate the presence of agent

in disrupted samples as well as in living cells (4, 17). GT cells also

may be used for testing infectivity of viral nucleic acids as well

as PrP conformers. Rapid assays of infectivity in culture should

facilitate the isolation of infectious particles from host components,

and treatments that modify the production of these

particles in culture may resolve further the infectious structure

from the pathological disease processes it initiates.

Materials and Methods......snip......end........TSS


http://www.pnas.org/cgi/content/abstract/0610999104v1




tss
 

PORKER

Well-known member
Well ,if its a virus ,BSE, then Ron you are a genius !!!!! That would mean that you could get BSE from eating veal or baby beef . All beef NEEDS TO be TESTED for BSE !!!!!!!!!!!!!!!!!!!!
 

rkaiser

Well-known member
Terry writes -
dang rkeiser, if you are refering to the fact the TSE ''agent'' as i have always said, which can survive ashing to 600 degrees C., and the fact that it would not matter if it was a prion or a virus or something in between, it's still one mean mother, if you are refering to that, i must give you more credit than you deserve

As usual one track terry can't read let alone listen

Quote-(from the article)

Quote:
"The human stomach and intestines would quickly break down any protein, normal or abnormal, before it reached the blood or brain, said Sheldon Penman, an emeritus professor of biology at Massachusetts Institute of Technology. "


I believe the fellow is debunking the whole "transmission and digestion of prion theory" Terry.
 

S.S.A.P.

Well-known member
Porker, the only thing I'm getting is a vision of what would happen to you if you made that statement in a room full of cattleman ....
 

PORKER

Well-known member
We cattlemen have given this a serious thought,compare this with tainted spinach that was recalled because one portion of one field was e-coli laden. They ,FDA ,recalled the whole country including Canada and we don't need this in the cattle industry.
 
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