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Targeted enzymatic therapy for coeliac disease
Marina Girbal-González1,2, Arturo Rodríguez-Banqueri3, Hadeel Swaid3,4
1Section of Physiology; Department of Biochemistry and Physiology; Faculty of Pharmacy and Food Sciences; University of Barcelona, Av. Joan XXIII, 27-31, 08028, Barcelona, Catalonia, Spain.
EMBO Molecular Medicine
|May 14, 2026
Summary
A novel enzyme, celiacase (Clc), effectively degrades gluten peptides in the stomach, offering a potential new therapy for celiac disease (CD) beyond a strict gluten-free diet.
Area of Science:
- Biochemistry
- Immunology
- Gastroenterology
Background:
- Celiac disease (CD) is an autoimmune disorder triggered by gluten peptides.
- Current management relies on a strict gluten-free diet, which has limitations.
- No curative therapies are currently available for CD.
Purpose of the Study:
- To develop and characterize a novel enzyme, celiacase (Clc), for gluten degradation.
- To evaluate the efficacy of Clc in preclinical models of celiac disease.
Main Methods:
- Engineered a recombinant prolyl endopeptidase (celiacase) from pitcher plant neprosin.
- Assessed Clc activity in simulated gastric conditions and against gluten peptides.
- Tested Clc in ex vivo assays with immune cells and patient biopsies.
- Evaluated Clc's therapeutic potential in vivo using a mouse model of gluten-induced enteropathy.
Main Results:
- Celiacase demonstrated optimal activity at gastric pH and efficiently cleaved immunogenic gluten peptides.
- Clc significantly reduced gluten peptide levels in a human gastrointestinal simulator.
- Clc-digested gluten failed to induce immune responses in macrophages and CD patient biopsies.
- In vivo, Clc treatment attenuated gluten-induced pathology, inflammation, and immune responses in mice.
Conclusions:
- Celiacase is a potent, acid-stable enzyme capable of degrading gluten immunogenic peptides.
- Clc shows promise as a therapeutic adjunct or alternative to a gluten-free diet for celiac disease patients.
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