On June 10, 2008 the scientific journal "Vaccine" published a paper by the Massachusetts based biotech company Cure Lab, Inc., demonstrating that a protein sequence important in neurodegenerative Huntington's disease can be safely used as a new generation of vaccine adjuvants.
The major component of every vaccine is an antigen that elicits specific immunity to a particular virus, bacteria or even cancer cells. Search for better antigens is one of the most pressing medical and public health necessities, and the biotech industry invests heavily in this research. However, antigens are able to generate a limited immune response if administered alone. In order to be protective or therapeutic, vaccine compositions have to be supplemented with adjuvants, strong facilitators of the immune response. In the search for efficient adjuvants that are also non-toxic, scientists at Cure Lab, Inc. discovered a novel paradigm that capitalizes on insights from recent breakthroughs in understanding the fatal neurodegenerative disorder, Huntington's.
Huntington's disease results from mutations in the protein huntingtin, which contains a sequence of polyglutamine residues (polyQ). In healthy individuals, huntingtin contains less than 35 glutamines in the polyQ segment. However, in neurons of Huntington's patients, the number of glutamine residues in the sequence expands to more than 36. This induces protein self-aggregation, or formation of big protein "chunks", and eventually causes neuronal dysfunction. Recent research findings indicate that attachment of a prolonged polyQ segment to almost any protein promotes its aggregation.
"There were two ideas - said Alex Shneider, Cure Lab's founder and CEO- which stimulated us to test if attachment of a long polyQ "tail" to an antigen can enhance immune response to vaccination". First, he noticed that small aggregates formed by an antigen fused to a polyQ tail resembled the droplets that convention
|Contact: Alex Shneider|
Cure Lab, Inc.