New molecule against celiac disease: celiacase breaks down gluten in the stomach

Catalan researchers develop an enzyme inspired by a carnivorous plant that could be a nutritional supplement for celiacs.

Representation of an enzyme molecule breaking down gluten.
IA

Representation of an enzyme molecule breaking down gluten.

An innovative molecule, celiacase, developed by researchers in Barcelona, promises to be the first therapy for celiac disease, breaking down gluten in the stomach.

A molecule inspired by the digestive system of a carnivorous plant, Nepenthes ventrata, could change the lives of people with celiac disease. Named celiacase, this enzyme has the ability to break down gluten during the early stages of digestion, opening a new therapeutic avenue for this autoimmune condition.
The research, jointly led by the Institute of Molecular Biology of Barcelona of the CSIC, the Research Institute of Nutrition and Food Safety (INSA), and the Faculty of Pharmacy and Food Sciences of the UB, focuses on an autoimmune disease triggered by the consumption of gluten and other prolamins found in cereals.
According to F. Xavier Gomis-Ruth, a research professor at IBMB-CSIC, celiacase functions effectively in an acidic environment like the stomach. Its action involves breaking down gluten before it reaches the intestine, thereby preventing the autoimmune inflammatory response characteristic of celiac disease and helping intolerant individuals digest food better.
The future vision is for celiacase to be marketed as a nutritional supplement, not a medication. Currently, the only therapeutic alternative for individuals with celiac disease or gluten intolerance is to follow a strict diet free of this protein, found in cereals such as wheat, barley, and rye.
Francisco J. Pérez Cano, director of INSA at the University of Barcelona, highlights the importance of this enzyme for situations where a celiac person might accidentally ingest traces of gluten, for instance, in a restaurant. Celiacase would act as a complement to the diet, counteracting the potential effects of unintentional intake and providing greater security.
Pre-clinical trials, conducted with a digestive system simulator and in models of celiac mice, have demonstrated the efficacy of celiacase. The enzyme was capable of almost completely degrading gluten in the stomach, preventing potentially harmful proteins from reaching the intestine and causing adverse effects. Treated mice managed to avoid typical disease biomarkers, such as microbiota alterations.
The research team is now in a crucial phase to verify if this efficacy holds true in humans through clinical trials. Concurrently, efforts are underway to establish a spin-off company to advance the project's development. If safety tests are positive and the molecule proves effective in humans, it could be available on the market within two to three years.