ArticleNature communications2022
Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- The protease code of the bacterial gut microbiota: ecological regulation, barrier disruption, and rewiring host defense and signaling.Gut microbes · 2026Review
- The plasma metabolome and clinical features of patients with coeliac disease in Northwest China.Annals of medicine · 2026Article
- Harnessing gut microbiome enzymes:Microbiology spectrum · 2026Article
- Targeted enzymatic therapy for coeliac disease.EMBO molecular medicine · 2026Article
- Jasmonate signaling and prey nutrient availability trigger distinct biochemical responses in the Drosera capensis feeding cycle.Plant physiology · 2026Article
- The Adaptable Binding Cleft of RmuAP1, a Pepsin-like Peptidase fromBiomolecules · 2025Article
- HemPepPred: Quantitative Prediction of Peptide Hemolytic Activity Based on Machine Learning and Protein Language Model-Derived Features.Foods (Basel, Switzerland) · 2025Article
- Impacts of conditionally essential amino acids, cysteine, and tyrosine on intestinal inflammation in celiac disease.Amino acids · 2025Review
- Is There a Future Without Gluten Restrictions for Celiac Patients? Update on Current Treatments.Nutrients · 2025Review
- Review Article: Novel Enzyme Therapy Design for Gluten Peptide Digestion Through Exopeptidase Supplementation.Alimentary pharmacology & therapeutics · 2025Review
- Postproline Cleaving Enzymes also Show Specificity to Reduced Cysteine.Analytical chemistry · 2024Article
- Specificity Enhancement of Glutenase Bga1903 toward Celiac Disease-Eliciting Pro-Immunogenic Peptides via Active-Site Modification.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The digestion of gluten generates toxic peptides, among which a highly immunogenic proline-rich 33-mer from wheat α-gliadin, that trigger coeliac disease. Neprosin from the pitcher plant is a reported prolyl endopeptidase. Here, we produce recombinant neprosin and its mutants, and find that full-length neprosin is a zymogen, which is self-activated at gastric pH by the release of an all-β pro-domain via a pH-switch mechanism featuring a lysine plug. The catalytic domain is an atypical 7+8-stranded β-sandwich with an extended active-site cleft containing an unprecedented pair of catalytic glutamates. Neprosin efficiently degrades both gliadin and the 33-mer in vitro under gastric conditions and is reversibly inactivated at pH > 5. Moreover, co-administration of gliadin and the neprosin zymogen at the ratio 500:1 reduces the abundance of the 33-mer in the small intestine of mice by up to 90%. Neprosin therefore founds a family of eukaryotic glutamate endopeptidases that fulfils requisites for a therapeutic glutenase.
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