As federal and state government officials grapple with strategies to limit the economic and health risks associated with the troublesome discovery of the nation's first case of Bovine Spongiform Encephalopathy (BSE) or "Mad Cow Disease"-- Will Eyestone, research associate professor in Large Animal Clinical Sciences, and Bill Huckle, associate professor of biomedical science, are conducting important research with the little understood molecules believed to cause the deadly brain-wasting disease.

Eyestone, a molecular reproductive biologist who was senior research scientist for PPL Therapeutics, the organization that cloned Dolly the sheep, now heads the VMRCVM's transgenic animal research program.

Most people think of disease as being caused by infectious organisms like bacteria, viruses, rickettsia, protozoa or fungi, explains Eyestone. Those microorganisms reproduce themselves to cause disease in fairly conventional ways, either inside a cell or elsewhere in the body.

But prions behave very differently than these more common disease-causing organisms, explains Eyestone. Prions are actually a form of protein that naturally occur in all mammals, though scientists remain uncertain about the exact purpose they serve in advanced mammals like humans. Transmissible spongiform encephalopathies like BSE and new variant Creutzfeldt-Jacob Disease (vCJD), the human form of the disease, are believed to occur when the non-pathogenic prions that normally reside in mammalian nervous systems are converted into pathogenic forms.

Proteins, the building blocks of metabolic processes, are long chains of amino acids that fold in upon themselves in predictable patterns and shapes that result from the bio-electrical relationships that exis
'"/>

Contact: Jeff Douglas
jdouglas@vt.edu
540-231-7911
Virginia Tech
8-Jan-2004