# Trimeric superoxide dismutase 1 antibody as a universal biomarker for ALS

## TL;DR

A new antibody can detect a toxic protein form linked to ALS, offering a specific diagnostic tool for the first time.

## Contribution

A novel synthetic antibody that specifically detects trimeric SOD1, a toxic protein form associated with ALS.

## Key findings

- The antibody binds selectively to trimeric SOD1 and distinguishes ALS patients from healthy individuals and those with other neurodegenerative diseases.
- The trimeric SOD1 is a shared pathological signature in ALS patients, even those without genetic mutations.
- This discovery provides the first disease-specific diagnostic tool for ALS.

## Abstract

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease that leads to the loss of motor neurons, resulting in paralysis and death. Currently, there are no specific biomarkers available for diagnosing ALS. As a result, diagnosis currently relies on excluding other conditions, which forces patients to endure months or even years of uncertainty. The absence of a specific, reliable diagnostic tool has hindered both early intervention and therapeutic progress. Here we develop a novel synthetic antibody that can detect a toxic form of a known protein linked to ALS. This trimeric assembly of superoxide dismutase 1 (SOD1) is a soluble, structurally distinct oligomer that is highly toxic in cell models. The antibody selectively binds this trimer and differentiates individuals with the disease from healthy people and from those with other neurodegenerative diseases (Alzheimer’s and Parkinson’s disease). This breakthrough provides the first disease-specific diagnostic tool for this condition and reveals a shared pathological signature across patients, even in cases without genetic mutations. After decades without a specific diagnostic tool, this antibody signifies a long-awaited breakthrough, finally offering clinicians and researchers a reliable window into ALS pathology.