A report in the Sept. 27 issue of Science identifies the culprit inducing celiac sprue as a 33-mer peptide of gluten, and a bacterial prolyl endopeptidase which can metabolize this peptide both in vitro and in vivo as a potential strategy for oral supplement therapy.
“When I do presentations about the disease, typically the response I get is, ‘Who is Celiac Sprue?’ ” author Chaitan Khosla, from Stanford University in Palo Alto, California, says in a news release. “This disease has been overlooked in a very serious way by the basic science, clinical, and pharmaceutical communities.”
Khosla’s group performed a combined chemical, physiological, and immunological analysis of gluten proteins called gliadins, and they isolated a single component that triggers the autoimmune response characteristic of celiac sprue. The offending peptide is a chain of 33 amino acids resistant to metabolism by the human gastrointestinal tract. However, research on bacterial digestive enzymes identified a prolyl endopeptidase that can break the chain into innocuous components.
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