With this important discovery, published in the prestigious journal of the European Federation of Biochemical Societies, FEBS Letters, the UAB scientists have opened up a possible area of treatment for such diseases, and for improvement of bio-industrial protein recovery processes.

Proteins are long chains of amino acids which may refold and take on a variety of different shapes. In living organisms, proteins develop vital functions for the regulation of an infinite number of processes. The function of each protein is closely connected to its shape -- that is, how it is folded.

If proteins lose their original shape, they also lose their functionality. In spongiform encephalopathies, including BSE (Mad Cow Disease), scrapie in sheep, and Creutzfeldt-Jacob disease in humans, the action of prions leads to large aggregations of proteins which lose their original shape and, therefore, their functionality.

A research team from the Institute of Biotechnology and Biomedicine of Universitat Autònoma de Barcelona, led by professor Antonio Villaverde, has discovered that the formation of aggregations of proteins found in bacteria -- the so-called inclusion bodies -- is reversible.

This means that under certain conditions, the proteins of an aggregate can recover their original shape and function, with complete disintegration of the aggregate.

The researchers have shown that disintegration of the protein aggregates may occur spontaneously through the action of cellular mechanisms which play a role in protein refolding.

This unexpected discovery opens the door to possible applications for the treatment of spongiform encephalopathies and, indeed, all diseases whose origin lies in the formation of protein aggregates and the resulting loss of functionality: familial fatal insomnia, Gerstmann-Sträussler-Scheinker syndrome and non-prionic amyloidosis such as Alzheimer's disease, Huntington's disease, type II diabetes and various muscular and spino-cerebellar atrophies.

Furthermore, controlled dissolution of protein aggregates also offers great scope for fabrication of proteins by means of bacteria, since the formation of inclusion bodies is one of the main obstacles to such processes. The UAB researchers have patented a method for protein recovery based on aggregate dissolution, which will soon find application in the bio-industrial production sector.

(Reference: FEBS Letters 489 (2001) 29-33.)

[Contact: Antonio Villaverde]

02-Mar-2001