A Taste of Wellness for Savoury and Snacks
Givaudan
Australian company Gradipore claims that it has developed a new technology to remove the protein that causes mad cow and other neuro-degenerative diseases from blood samples.
According to the company, its Gradiflow technology has been proven to successfully concentrate and remove infectious and non-infectious prion proteins from human biological samples in laboratory studies.
The advance is the result of experiments designed, performed and validated in collaboration with the Scottish National Blood Transfusion Service (SNBTS) and Q-One Biotech, an independent authority in the design and implementation of virus, prions and other contaminant validation studies.
The potential for risks associated with infectious prion proteins in human biological products is of current concern the world over. These agents cause the transmissible spongiform encephalopathy (TSE) diseases such as Scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and Variant Creutzfeldt-Jakob disease (vCJD) in humans.
A major challenge of TSE diseases is to develop a fast, sensitive and reliable diagnostic test to detect the presence of infectious prion proteins at an early stage of the disease. Technology currently exists to detect the presence of infectious prions post-mortem, or after cattle have been slaughtered.
However, this process is time consuming, and due to necessary test-related lead times, can allow the disease to spread before the condition is discovered. The development of a diagnostic test for livestock that can detect infectious prions in vivo (in live subjects), could expedite discovery of possible disease and represents a market opportunity of up to approximately US $2.5 billion for cattle and sheep populations in the countries of the European Union alone.
SNBTS has a standing agreement with Gradipore , originally announced in November 2001, for the development of Gradiflow, a scaleable technology that can successfully purify and decontaminate plasma proteins as well as concentrate prion proteins in human blood samples.
In addition to the study of Gradiflow in prion protein removal, the threefold agreement also covers the development of an infectious prion protein diagnostic tool for early stage detection of prion disease.
"We are very encouraged by the results of these experiments. The outcome of this collaborating project could allow early prion diagnosis, limit the potential of TSE further transmission and possibly assist in treatment of TSE disease," said Robert Lieb, global CEO for Gradipore. "Indeed, what they show is that Gradiflow may fill the unmet need for a non-invasive prion diagnostic tool for animals and humans, and can provide pure isolates of various proteins useful for research, development, and therapeutic purposes."