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Early tests suggest that therapy with a combination of two enzymes inactivates gluten in the gut and may someday benefit patients with celiac disease.
In two papers appearing in the journal Chemistry and Biology, Dr. Chaitan Khosla and colleagues, from Stanford University in California, describe the creation of this oral enzyme therapy, which they believe could alleviate many of the symptoms and complications of celiac sprue.
First, the researchers explain that they genetically engineered EP-B2, an enzyme found in barley seeds. They then created a compound in which EP-B2 was attached to Escherichia coli, a bacterium normally present in the gut that is frequently used to transport the active agent in gene therapies. Further testing of the EP-B2/E. coli compound showed that it efficiently inactivated a wheat gluten protein at regions toxic to celiac disease patients.
In the second study, EP-B2, which works under the gastric conditions that exist in the stomach, was coupled with a prolyl endopeptidase (PEP), an anti-gluten enzyme that functions in the intestines. Testing of this compound under conditions that simulated the intestines resulted in rapid and complete detoxification of grocery store gluten.
“Non-dietary therapies that allow celiac patients to safely incorporate low-to-moderate levels of gluten into their daily diet would be of considerable benefit,” Khosla said in a statement.
The researchers note that gluten is in many products, but food labels are often inaccurate and don’t mention gluten as an ingredient. “Our results suggest that recombinant EP-B2 should be effective as supportive therapy to help celiacs cope with the ‘hidden’ gluten in everyday life,” Khosla said. This new “two-enzyme cocktail” of EP-B2 and PEP may eventually permit patients with celiac disease eat a more normal diet.