New Enzyme "Celiacase" Shows Promise in Breaking Down Gluten in the Stomach
A research team has successfully designed a molecule that degrades gluten immunogenic peptides (GIPs) at the acidity level of the human stomach, potentially offering a new avenue for treating coeliac disease.
The Challenge
For individuals with coeliac disease, even trace amounts of gluten can trigger severe intestinal damage, inflammation, and long-term health complications. Current treatment relies entirely on strict, life-long avoidance of gluten.
The Breakthrough
A collaboration between the Institute for Research in Nutrition and Food Safety (INSA), the Faculty of Pharmacy and Food Sciences at the University of Barcelona, and the Molecular Biology Institute of Barcelona (IBMB) (CSIC), has led to a novel solution.
What is Celiacase?
The molecule, named celiacase, is engineered from a naturally occurring enzyme called nephrosin, which is found in the carnivorous plant Nepenthes ventrata.
- Designed for the Stomach: Celiacase was specifically engineered to remain active at pH 2, the high acidity level of the human stomach. This is where gluten first becomes a problem.
- Targeted Action: The molecule effectively degrades gluten immunogenic peptides (GIPs) directly in the stomach.
- Self-Limiting: Crucially, celiacase naturally becomes inactive after it reaches the duodenum, reducing the risk of unintended effects on digestion further down the tract.
Evidence in Mouse Models
In a mouse model of coeliac disease, treatment with celiacase yielded positive results at low doses.
"Celiacase reduced intestinal atrophy, inflammation, antibody response, and dysbiosis at low doses."
This suggests the molecule can prevent the hallmark cascade of immune reactions and tissue damage caused by gluten exposure.
Future Outlook
The research findings have been published in EMBO Molecular Medicine. The team has already secured a patent for celiacase and is actively pursuing a spin-off company to oversee further development and potential clinical testing.