New Biology Economy

New Biology Economy tracks news of the emerging molecular biology tools marketplace, which is building on foundational biotechnical advances to create new insights into complex biological systems. This blog begins with the understanding that traditional business methods must change to enable innovation to create wealth and eventually benefit patients. This will require cooperation, new ways of protecting intellectual property, and will spawn new types of business organizations.

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Monday, August 29, 2005

Paper Describes New Prion Amplification Technology for Blood Testing Applications

  • Researchers at the University of Texas Medical Branch at Galveston say that within six months they expect to have an early-stage technology to test human blood for the malformed proteins that cause new-variant Creutzfeldt-Jakob disease, the human form of Bovine Spongiform Encephalopathy or mad cow disease, according to a paper published in the journal Nature Medicine this week.

    New-variant Creutzfeldt-Jakob disease is believed to be caused by humans eating neural tissue, such as brain and spinal cord, from BSE-affected cattle.

    The Galveston researchers have developed a technique that detects the proteins in blood samples taken from hamsters. Their test, which amplifies the proteins in blood to a detectable level, takes days to complete.

    According to an article in Nature, the lead author of the study Claudio Soto, a University of Texas in Galveston neuroscientist, said the technology will need more testing. Additionally, there are ethical issues to resolve about screening for a disease that has no known cure. "That's an important question that someone has to resolve," Soto said.

    Mad cow disease is an evolving food security concern. Two cases of the disease have been confirmed in US cows and currently the only way to test for it is in a post-mortem proceedure in animals.

    Bio-Rad of Hercules, Calif., is the market leader in testing for Bovine Spongiform Encephalopathy.

    The company provides an ELISA test, a process in which brain material is homogenized, with normal prion protein being destroyed by a protease, and any remaining abnormal prion protein bound to the surface of a clear microtiter well and immunologically detected. The signal is detected by a spectrophotometer and results are output in a quantitative format. This testing procedure takes four hours to complete. [See New Biology Economy, Aug. 5.]

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