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By stitching together segments of two species of infectious yeast proteins, called prions, researchers have produced a hybrid prion that can adopt two distinct infectious shapes.
This ability to change conformation allows the hybrid prion to bridge a species barrier and "infect" proteins from two distantly related species of yeast. This phenomenon, say the scientists, may be a key to understanding how prions derived from cows infected with bovine spongiform encephalopathy (BSE), or "mad cow disease," can hop the species barrier and infect humans.
The scientists conducted their studies using yeast prions, which are similar to the mammalian prions that have gained notoriety for their roles in such fatal brain-destroying human diseases such as Creutzfeldt-Jakob disease and kuru, and in the animal diseases BSE and scrapie.
Both yeast and mammalian prions are proteins that transmit their characteristics via protein-protein interactions in which an abnormally shaped prion protein influences its normal counterpart to assume an abnormal shape. In mammalian prion infections, abnormal, insoluble shapes trigger protein clumping that can kill brain cells. In yeast cells, the insoluble prion protein is not deadly; it merely alters a cell's metabolism.
Are prions the same thing as bacteria or viruses?
No. Unlike viruses and bacteria, prions lack nucleic acid, a vital component of living cells. They're also nearly indestructible — impervious to heat, radiation, washing, boiling and strong chemicals, including stomach acid.
The most likely means of transmission is between animals that are in close contact with each other.