Novel aciduric gluten-degrading enzyme promising in celiac disease
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Researchers have identified the novel enzyme, pseudolysin, from Pseudomonas aeruginosa, as a potential novel treatment for celiac disease, according to study results.
“Identification of an enzyme with activity at low pH is highly desired from a therapeutic perspective, as it would enable gluten digestion during gastric passage, before immunogenic epitopes reach the duodenum, where immune destruction begins. Such activities are of particular interest if they are associated with natural colonizers of the gastrointestinal tract,” Guoxian Wei, DDS, MS, PhD, of the department of molecular and cell biology at the Henry M. Goldman School of Dental Medicine in Boston, and colleagues wrote.
Wei and colleagues sought to identify microorganisms with gluten-degrading properties from the human feces of three healthy participants.
Of the 278 strains obtained from the fecal samples, 127 were cultured in aerobic conditions and 151 were cultured in anaerobic conditions. There were 93 gathered on gluten agar (GA) plates at pH 4 and 185 from GA plates at pH 7.
When the researchers tested strains FA-10 and FA-13 for gliadin degradation at pH 7, 4 and 2, gliadins were effectively cleaved by cell-associated protease for both FA-10 and FA-13 at pH 7 and pH 4.
Twenty-two of 43 active strains were identified by the researchers as P. aeruginosa, for which degradation of gliadin occurred between pH 2 and pH 7. Results of an analysis with liquid chromatography-electrospray ionization-tandem mass spectrometry identified the pseudolysin enzyme.
“Pseudolysin was identified as an enzyme cleaving gluten effectively at extremely low as well as near-neutral pH values,” Wei and colleagues wrote. “The potential to degrade gluten during gastric transport opens possibilities for its application as a novel therapeutic agent for the treatment of celiac disease.” – Jennifer Southall
Disclosure: The researchers report no relevant financial disclosures.