I’ve received several email messages asking about prion frequencies. The current epidemic flu produces proteins which appear to be susceptible to frequencies, so it ought to be possible to knock out a prion. I’ve responded that without a test case, or better yet, a set of test cases, it is difficult to identify frequencies, assess whether there are various strains that require different frequencies, or whether the DNA structure varies across individuals.
In any event, microscopic photos are a good source of candidate frequencies. The frequency of the prion in the image below is 5654.24hz. A number of proteins seem to respond well to frequencies in the 5000-7000hz range. This is an area which obviously needs a lot more study.
Microscopic image of a tissue sample from a human brain that shows a clump of infectious prions (dark pink area).
Image: Dr.Neil Cashman, University of Toronto
Possible diagnosis, treatment, vaccine for mad cow, prion diseases found
Raising antibodies against tyrosine-tyrosine-arginine amino acid sequence the key
by Janet Wong, University of Toronto, 4 Jan 2004
June 2, 2003 — Research led by scientists at the U of T and Caprion Pharmaceuticals has uncovered the basis for a diagnostic, immunotherapy and vaccine, providing a way to detect and treat the brain-wasting damage of infectious prions like those found in mad cow disease and its human version, Creutzfeldt-Jakob Disease.
Dr. Neil Cashman, a principal investigator at U of T’s Centre for Research in Neurodegenerative Diseases and professor in the Department of Medicine (neurology) and a Caprion founder, says a vaccine approach – which would likely be of most use in animals and livestock – could prevent animals from becoming infected. For humans with diseases like classical or variant Creutzfeldt-Jakob, an immunotherapeutic would provide patients with antibodies that bind infectious prions, enabling the immune system to recognize and attack them. For both humans and animals, the diagnostic screening potential of this discovery could significantly improve the safety of the human blood and food systems.
Cashman, who also holds the Jeno Diener Chair in Neurodegenerative Diseases at U of T, says his team tried a new approach in studying infectious prions, which are particles thought to be composed of normal prion proteins that have been compromised and folded into rogue shapes. “The usual way of raising antibodies in the immune system is to grind the infectious agent up and inject it into a mouse to see if it prompts antibody production,” he says. “Scientists have tried this method with prions over the past 15 years, all without success. My group decided to examine it from the sub-molecular level to determine if antibodies would recognize and react to the amino acids exposed at the surface of a prion. It was a novel idea, and when we found that our hypothesis actually worked, we were surprised and pleased.” The researchers’ findings are reported online in the June 1 version of Nature Medicine.
All mammals have prion proteins, the highest levels of which are present in the brain, explains Cashman, a senior scientist at Sunnybrook and Women’s Research Institute and a neurologist in the Department of Medicine at Sunnybrook and Women’s College Health Sciences Centre. Mammals can contract prion diseases by ingesting abnormal or infectious prions. From the digestive system, these prions make their way to the brain. When an abnormal prion comes in contact with a normal prion protein, it causes the protein to misfold, thus creating a copy of the infectious prion. Cashman says the process is more akin to co-opting than replication. However, since the abnormal prion has similar characteristics to the original host protein, the immune system does not recognize it as a foreign invader and does not attack it.