Abstract
To date, there is no effective treatment for celiac disease (CD, gluten enteropathy), an autoimmune disease caused by gluten-containing food. Celiac patients are supported by a strict gluten-free diet (GFD). However, in some cases GFD does not negate gluten-induced symptoms. Many patients with CD, despite following such a diet, retain symptoms of active disease due to high sensitivity even to traces of gluten. In addition, strict adherence to GFD reduces the quality of life of patients, as often it is difficult to maintain in a professional or social environment. Various pharmacological treatments are being developed to complement GFD. One promising treatment is enzyme therapy, involving the intake of peptidases with food to digest immunogenic gluten peptides that are resistant to hydrolysis due to a high prevalence of proline and glutamine amino acids. This narrative review considers the features of the main proline/glutamine-rich proteins of cereals and the conditions that cause the symptoms of CD. In addition, we evaluate information about peptidases from various sources that can effectively break down these proteins and their immunogenic peptides, and analyze data on their activity and preliminary clinical trials. Thus far, the data suggest that enzyme therapy alone is not sufficient for the treatment of CD but can be used as a pharmacological supplement to GFD.
Highlights
Celiac disease (CD), or gluten enteropathy, is a hereditary predisposed disease, accompanied by the atrophy of the small intestine mucosa, associated malabsorption syndrome, and the development of various deficiency conditions [1,2]
ImmunogenX, a clinical biotherapy company, has published the results of phase 2 trials of latiglutenase [72]. These results demonstrated that latiglutenase was safe and effective in reducing the symptoms of seropositive CD patients on a gluten-free diet
Hydrolysis of proline/glutamine-rich proteins is difficult because most broad-spectrum peptidases are unable to cleave the peptide bonds formed by proline and glutamine residues
Summary
Celiac disease (CD), or gluten enteropathy, is a hereditary predisposed disease, accompanied by the atrophy of the small intestine mucosa, associated malabsorption syndrome, and the development of various deficiency conditions [1,2]. Pharmaceutics 2021, 13, 1603 immunogenic peptides formed from them, are rich in proline, which is the only imino acid among the twenty natural proteinogenic amino acids. The ability of PSPs to neutralize the immunogenic potential of proline-rich gluten peptides is a way to exploit their unique specificity and presents an attractive option for patients with CD. Oral enzyme therapy using such gluten-destroying peptidases is a promising therapeutic approach This narrative review describes the features and characteristics of the main proline/glutamine-rich proteins of cereals, analyzes peptidases from various sources that can effectively break down these proteins, and discusses their potential to produce gluten-free products, including the problems in incorporating these enzymes in therapies for CD
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