In vitro Gluten Degradation Using Recombinant Eurygaster Integriceps Prolyl Endoprotease: Implications for Celiac Disease

Celiac disease (CD) is a gluten-sensitive chronic autoimmune enteropathy. A strict life-long gluten-free dietis the only efficient and accepted treatment until now. However, maintaining a truly gluten-free status is both difficult and costly, often resulting in a social burden for the person. Moreover, 2 to 5 percent of patients fail to improve clinically and histologically upon elimination of dietary gluten. Therefore, novel therapeutic approaches, including gluten degrading enzymes, are an unmet need of celiac patients.

To evaluate the function of sunn pest prolyl endoprotease for gluten and gliadin hydrolysis in vitro.

The spPEP was expressed as a recombinant protein in E. coli BL21 (DE3), and its catalyticactivity was assessed by SDS-PAGE and RP-HPLC analyses.

Production of a 100-kDa spPEP protein was confirmed by SDS-PAGE and western blot analysis. Also, wedemonstrate that spPEP efficiently degrades gluten and α-gliadin (30-40 kDa) in vitro under conditions similar to the GIand is resistant to pepsin and trypsin.

The gathered data demonstrated that spPEP might be a novel candidate for Oral Enzymatic Therapy (OET)in CD and other gluten-related disorders.