Gluten Immunogenic Peptides as Standard for the Evaluation of Potential Harmful Prolamin Content in Food and Human Specimen

Cebolla, Ángel; Moreno, María de Lourdes; Coto, Laura; Sousa, Carolina

doi:10.3390/nu10121927

Cited by 64 publications

(38 citation statements)

References 107 publications

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“…34,69 Two peptides that have attracted most attention and remain intact in the digestive process are the 33-mer (p55-87) and the 25-mer (p31-55) located in the αgliadins encoded by the Gli-D2 locus on chromosome 6D. 73,74 Of these two peptides, the 33-mer is the most digestion-resistant peptide with high immunogenic properties (contains DQ2.5-glia-α1a, DQ2.5-glia-α1b, and DQ2.5-glia-α2 epitopes). 75,76 During or after absorption of partially digested gliadin peptides into the lamina propria, specific glutamine residues of the 33-mer peptide are susceptible to pH-dependent transamidation (covalent cross-linking to free amines, for example, lysine residues submit your manuscript | www.dovepress.com…”

Section: Gluten Protein and The Pathogenesis Of Various Grds Celiac Dmentioning

confidence: 99%

The Gluten Gene: Unlocking the Understanding of Gluten Sensitivity and Intolerance

Asri¹,

Rostami-Nejad²,

Rostami³

2021

TACG

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Wheat flour is one of the most important food ingredients containing several essential nutrients including proteins. Gluten is one of the major protein components of wheat consisted of glutenin (encoded on chromosome 1) and gliadin (encoded on chromosome 1 and 6) and there are around hundred genes encoding it in wheat. Gluten proteins have the ability of eliciting the pathogenic immune responses and hypersensitivity reactions in susceptible individuals called “gluten-related disorders (GRDs)”, which include celiac disease (CD), wheat allergy (WA), and non-celiac gluten sensitivity (NCGS). Currently removing gluten from the diet is the only effective treatment for mentioned GRDs and studies for the appropriate and alternative therapeutic approaches are ongoing. Accordingly, several genetic studies have focused on breeding wheat with low immunological properties through gene editing methods. The present review considers genetic characteristics of gluten protein components, focusing on their role in the incidence of gluten-related diseases, and genetic modifications conducted to produce wheat with less immunological properties.

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Section: Gluten Protein and The Pathogenesis Of Various Grds Celiac Dmentioning

confidence: 99%

The Gluten Gene: Unlocking the Understanding of Gluten Sensitivity and Intolerance

Asri¹,

Rostami-Nejad²,

Rostami³

2021

TACG

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“…Although growth and gliadin hydrolysis plating approach is an appropriate initial step for the selection of microorganisms capable of utilizing gluten, highly active gluten-degrading enzymes nor specificities of interest targeting immunogenic domains are not necessarily produced and exhibit by the isolated strains [34]. Therefore, further evaluation was required to check the reduction of gluten immunogenic peptides (GIP) by the selected strain since the detection of GIP has been proposed as the analytical standard reference for the determination of the immunopathological risk of gluten exposure in gluten-related diseases [35].…”

Section: Resultsmentioning

confidence: 99%

“…Previous reports have demonstrated that the G12 moAb specifically recognizes the immunoreactive peptides in those gluten proteins that have a reported characterization of the consistency with ex-vivo -quantified immunogenicity with T-cells from celiac individuals [35–39]. To monitor GIP hydrolysis, microbial encapsulation in monodisperse hydrogel gliadin microspheres was performed with Cellena Flow Focusing technology (Ingeniatrics).…”

Section: Resultsmentioning

confidence: 99%

A new microbial gluten-degrading prolyl endopeptidase: Potential application in celiac disease to reduce gluten immunogenic peptides

et al. 2019

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Gluten is a complex of proteins present in barley, wheat, rye and several varieties of oats that triggers celiac disease in genetically predisposed subjects. Gluten is notoriously difficult to digest by mammalian proteolytic enzymes and therefore, proline-rich digestion-resistant peptides contain multiple immunogenic epitopes. Prolyl endopeptidases (PEP) hydrolyse internal proline residues on the carboxyl side of peptides and have been proposed for food gluten detoxification and as oral enzyme supplementation for celiacs. The aim of this study was to identify new gluten-degrading microbial enzymes with the potential to reduce gluten immunogenicity by neutralizing its antigenic epitopes. Using a gluten-degrading colony screening approach, a bacterial isolate (2RA3) displaying the highest glutenase activity was selected, characterized and its genome completely sequenced. The identification through 16S rDNA gene sequencing showed a 99,1% similarity to Chryseobacterium taeanense . Hydrolysis of gluten immunogenic peptides (GIP) was further monitored, over a 48-hour period, by colony encapsulation in gliadin-containing microspheres, followed by detection with the G12 anti-GIP monoclonal antibody. Glutenase activity was detected in the extracellular medium of 2RA3 cultures, where gel electrophoresis and gliadin zymography revealed the presence of a ~50 kDa gluten-degrading enzyme. Nano-ESI-Q-TOF of the excised active band identified 7 peptides contained in the protein product predicted for an open reading frame (ORF) in the 2RA3 genome. Based on sequence similarity to the PEP family, the new enzyme was named PEP 2RA3. The PEP 2RA3 coding sequence was PCR-amplified from C . taeanense 2RA3, cloned and expressed in Escherichia coli as a C-terminally His-tagged recombinant protein and purified by Ni-NTA affinity chromatography. The recombinant protein, with predicted molecular mass and isoelectric point of 78.95 kDa and 6.8, respectively, shows PEP activity with standard chromogenic substrates, works optimally at pH 8.0 and 30°C and remains stable at pH 6.0 and 50°C, indicating a potential use in gluten-containing food process applications. The ability of the recombinant enzyme to degrade GIP in beer into smaller peptides was confirmed.

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“…GIP, analyzed in stools and urine by using commercial ELISAs (monoclonal antibodies G12 and/or A1), have been proposed as new non-invasive biomarkers to detect gluten intake and to verify GFD compliance in patients with CD [45,46,49,[80][81][82][83][84][85]. GIP are resistant to gastrointestinal digestion and responsible for immunogenic reactions in the T cells of patients with CD [83]. Unlike traditional methods for monitoring GFD adherence, which only evaluate the consequences of GFD transgressions, this non-invasive method enables a direct and quantitative assessment of gluten exposure.…”

Section: Stools and Urine Testingmentioning

confidence: 99%

Challenges of Monitoring the Gluten-Free Diet Adherence in the Management and Follow-Up of Patients with Celiac Disease

et al. 2021

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Celiac disease (CD) is a chronic gluten-responsive immune mediated enteropathy and is treated with a gluten-free diet (GFD). However, a strict diet for life is not easy due to the ubiquitous nature of gluten. This review aims at examining available evidence on the degree of adherence to a GFD, the methods to assess it, and the barriers to its implementation. The methods for monitoring the adherence to a GFD are comprised of a dietary questionnaire, celiac serology, or clinical symptoms; however, none of these methods generate either a direct or an accurate measure of dietary adherence. A promising advancement is the development of tests that measure gluten immunogenic peptides in stools and urine. Causes of adherence/non-adherence to a GFD are numerous and multifactorial. Inadvertent dietary non-adherence is more frequent than intentional non-adherence. Cross-contamination of gluten-free products with gluten is a major cause of inadvertent non-adherence, while the limited availability, high costs, and poor quality of certified gluten-free products are responsible for intentionally breaking a GFD. Therefore, several studies in the last decade have indicated that many patients with CD who follow a GFD still have difficulty controlling their diet and, therefore, regularly consume enough gluten to trigger symptoms and damage the small intestine.

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Gluten Immunogenic Peptides as Standard for the Evaluation of Potential Harmful Prolamin Content in Food and Human Specimen

Cited by 64 publications

References 107 publications

The Gluten Gene: Unlocking the Understanding of Gluten Sensitivity and Intolerance

The Gluten Gene: Unlocking the Understanding of Gluten Sensitivity and Intolerance

A new microbial gluten-degrading prolyl endopeptidase: Potential application in celiac disease to reduce gluten immunogenic peptides

Challenges of Monitoring the Gluten-Free Diet Adherence in the Management and Follow-Up of Patients with Celiac Disease

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