-Caveat Lector-

Euphorian spotted this on the Guardian Unlimited Observer site and thought you should 
see it.

To see this story with its related links on the Guardian Unlimited Observer site, go 
to http://www.observer.co.uk

Eating meat 'may still pose CJD risk'
Robin McKie, science editor
Saturday November 30 2002
The Guardian


Muscle and flesh of cattle and sheep may harbour deadly levels of prions that cause 
variant CJD. This stark prospect, raised by the Nobel Prize winner who first 
discovered that these infective particles can cause brain illnesses, suggests eating 
meat may still pose a serious health risk.

The prospect that a timebomb may still be ticking in our kitchens was raised by 
Stanley Prusiner, who revealed yesterday that experiments at the University of 
California in San Francisco had shown that scrapie-infected mice have unexpectedly 
high concentrations of prions in their muscles.

'These are just mouse models, but they raise the obvious worry that cows and sheep 
could be similarly affected,' said Prusiner, who received the 1997 Nobel Prize for 
medicine for discovering that degenerative brain diseases such as Creutzfeldt-Jakob 
Disease are caused by prions.

Until now, scientists had assumed that only brains and spinal columns of cows and 
sheep contain dangerous levels of prions. But it appears that cuts of beef and lamb, 
which largely consist of muscle, could also be affected.

'The levels we found were a hundredfold less than those found in brains, but were 
still   significant,' he said. 'In particular, we found that the hind legs of mice had 
high numbers of prions. It remains to be seen if that is mirrored in the hind legs of 
cattle or sheep.'

Prusiner said that part of the problem could be traced to existing tests for the 
existence of prions in animals or humans. 'These tests chew up prion molecules in such 
a way that means we fail to spot them. We were destroying critical evidence of 
infections, perhaps up to 99 per cent of it. It is very serious.'

As a result, he and his colleagues have perfected a new technique for detecting prions 
in samples, one that is 10,000 times more sensitive than existing tests used in Europe 
and America.

The new test - conformation dependent immunoassay (CDI) - works on a completely 
different principle. Essentially, it recognises the shape of prion molecules. 'We 
believe that by applying the test to cattle we should significantly reduce human 
exposure to bovine prions,' said Dr Jiri Safar, one of Prusiner's colleagues.

'Previous attempts to quantify BSE and scrapie prions in milk or non-neural tissue, 
such as muscle, may have underestimated infectious titers [levels] by as much as a 
factor of 10,000, raising the possibility that prions could be present in sufficient 
quantities to pose risk to humans. The high sensitivity of this new test may 
profoundly alter our view of the epidemiology of prion diseases.'

However, Prusiner had one reassuring message. He dismissed a study, published last 
week by British researcher John Collinge, which suggested that BSE was responsible for 
more than one type of CJD in this country. In the journal of the European Molecular 
Biology Organisation, Collinge suggests that a second form of the disease was also 
caused by prions from meat. However, Prusiner dismissed the idea. 'I simply do not 
read the data the way that he does. I can see no evidence of such an effect. I just 
don't think it is likely.'

Copyright Guardian Newspapers Limited

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