Antibody Developed to Detect Mutant Enzyme Causing Amyotrophic Lateral Sclerosis

Filed in archive Diagnostics, Methodologies and Instrumentation , Genomics, Proteomics and Bioinformatics on May 14, 2007

Amyotrophic lateral sclerosis (ALS), also called Lou Gehrig's disease, is a progressive and usually fatal neurological disorder that attacks the nerves and muscles. Researchers have now developed the first antibody that detects misfolded conformations of the enzyme superoxide-dimutase-1 (SOD1), which cause approximately one to two per cent of all ALS cases.

"This antibody will enable researchers to investigate whether misfolded SOD1 is involved in other forms of ALS. [snip] This is important to determining if SOD1 is relevant in ALS cases that are not caused by mutations in SOD1. If this is the case, then the antibody could potentially be used in biomarker studies to facilitate earlier diagnosis of the disease."

The antibody, named SOD1-exposed-dimer-interface antibody (SEDI-antibody), also opens up the possibility of developing immunization strategies for the treatment of ALS caused by SOD1 mutations. [snip] The SEDI antibody also has utility in drug discovery efforts for identifying chemical chaperones that prevent or reduce misfolding of SOD1 in ALS."

The study will be published in the June print edition of Nature Medicine.

Source: University of Toronto