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  • Jefferson Adams

    Breakthroughs in Synthetic Biology Driving Development of New Celiac Disease Treatments

    Jefferson Adams


    Reviewed and edited by a celiac disease expert.

      A team genetic engineering researchers at the University of Washington are developing a new treatment for celiac disease based on custom-designed enzymes that target gluten proteins. The result could be an oral enzyme therapy that dissolves gluten protein


    Caption: Image: CC--Nic Redhead

    Celiac.com 01/02/2019 - Way back in 2011, a team genetic engineering researchers at the University of Washington began to develop a new treatment for celiac disease. The team’s early research suggested that an oral enzyme that could break down the gluten proteins would be an ideal therapy for celiac disease. Taken before meals by a person with celiac disease, such an enzyme would ideally neutralize all trace of gluten before they could trigger an immune response. Their search to develop such a treatment would take them nearly a decade of effort.

    To fuel their goals, the team made use of pioneering computer software, called the Rosetta Molecular Modeling Suite, that helps design new proteins, including enzymes. They began by selecting a protein-digesting enzyme that was already known to work well in acidic conditions. However, the selected enzyme lacked the gluten-killing ability the team sought. Using a video game-like interface to Rosetta called Fold-it, the team created versions of the enzyme that would target gluten proteins. 



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    The team then chose about 100 of their most promising enzyme designs. They then physically created each of those designer enzymes in the lab and tested their ability to break down gluten. By combining the best performing enzymes, the team was able to create a prototype gluten-degrading enzyme, which they named KumaMax, as it is derived from the starter enzyme, kumamolisin. After years of additional tweaking of the prototype enzyme at the University of Washington’s Institute for Protein Design, the team was able to begin Phase I clinical trials on KumaMax.  

    If clinical trials go well, the team is looking to follow with testing on human celiac patients. The results could give rise to a new commercially available enzymatic treatment for celiac disease.

    Read more at: ASCH.ORG


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    Denatured Proteins,

    "Cooking" egg and/or "heating" milk proteins make these foods more easily digestible for those with egg and/or milk protein intolerance.

    Why is this not so with grain proteins such as gluten?

    At what temperature would a grain protein, such as modern dwarf wheat, become denatured?

    If the gluten is "digested" by enzymes, does the resulting "denatured" protein still continue to damage the bowel tissues as it travels along the small intestine?

    Can a "leaky" bowel heal despite repeated exposure to "denatured" gluten protein?

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  • About Me

    Jefferson Adams is Celiac.com's senior writer and Digital Content Director. He earned his B.A. and M.F.A. at Arizona State University, and has authored more than 2,500 articles on celiac disease. His coursework includes studies in science, scientific methodology, biology, anatomy, medicine, logic, and advanced research. He previously served as SF Health News Examiner for Examiner.com, and devised health and medical content for Sharecare.com. Jefferson has spoken about celiac disease to the media, including an appearance on the KQED radio show Forum, and is the editor of the book "Cereal Killers" by Scott Adams and Ron Hoggan, Ed.D.

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