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Link to original content: http://www.ncbi.nlm.nih.gov/pubmed/27763541
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Review
. 2016 Oct 18;8(10):644.
doi: 10.3390/nu8100644.

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

Anastasia V Balakireva  1 , Andrey A Zamyatnin  2   3
Affiliations
Review

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

Anastasia V Balakireva et al. Nutrients. .

Abstract

Theterm gluten intolerance may refer to three types of human disorders: autoimmune celiac disease (CD), allergy to wheat and non-celiac gluten sensitivity (NCGS). Gluten is a mixture of prolamin proteins present mostly in wheat, but also in barley, rye and oat. Gluten can be subdivided into three major groups: S-rich, S-poor and high molecular weight proteins. Prolamins within the groups possess similar structures and properties. All gluten proteins are evolutionarily connected and share the same ancestral origin. Gluten proteins are highly resistant to hydrolysis mediated by proteases of the human gastrointestinal tract. It results in emergence of pathogenic peptides, which cause CD and allergy in genetically predisposed people. There is a hierarchy of peptide toxicity and peptide recognition by T cells. Nowadays, there are several ways to detoxify gluten peptides: the most common is gluten-free diet (GFD), which has proved its effectiveness; prevention programs, enzymatic therapy, correction of gluten pathogenicity pathways and genetically modified grains with reduced immunotoxicity. A deep understanding of gluten intolerance underlying mechanisms and detailed knowledge of gluten properties may lead to the emergence of novel effective approaches for treatment of gluten-related disorders.

Keywords: NCGS; avenin; celiac disease; gliadin; gluten; gluten intolerance; glutenin; hordein; secalin; wheat allergy.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic representation of major pathways in celiac disease (CD) pathogenesis. MICA, NKG2D—stress molecules on enterocytes, IEL—intraepithelial lymphocyte, DC—dendritic cell.
Figure 2
Figure 2
Prolamin Superfamily composition.
Figure 3
Figure 3
Schematic representation of typical structure of prolamin group members: S-rich, S-poor, HMW and avenins. S—signal peptide; A, B, C—conserved regions, lines—disulfide bonds, red circles—unpaired cysteine residue, I2–I4—variant regions; parallel lines—contracted repetitive region. (A) Typical structure of S-rich prolamin. It contains conservative domains, repetitive region and is able to form intrachain disulfide bonds; (B) Typical structure of S-poor prolamin. It lacks conservative domains and cysteine residues, and is therefore not able to form any disulfide bonds; (C) Typical structure of HMW prolamin. It contains conservative domains, repetitive region and is able to form intra- and interchain disulfide bonds; (D) Typical structure of avenin. It contains conservative domains, repetitive regions and is able to form interchain disulfide bonds only.
Figure 4
Figure 4
Summary of evolutionary events that probably contributed to the divergence of Prolamin Superfamily proteins. A, B, C—conserved regions, S—signal peptide, I2–I4—variant regions. (A) Conservative domains A, B and C of prolamins are thought to originate from the ancestral domain by triplication. S-rich and HMW prolamins emerged after insertions of repetitive regions in a manner showed on a Figure; (B) S-poor prolamins are suggested to originate from S-rich prolamins by deletion of conserved A, B and C regions, and by multiplication of repeated sequences.
Figure 5
Figure 5
3D reconstruction of DQ α5-β2-binding cleft with a deamidated α-gliadin peptide (green), using PyMOL (PBD ID 1S9V) [81].
Figure 6
Figure 6
Fragment of α-gliadin protein sequence. Main immunogenic fragments: peptides p31-43, 33-mer and DQ2.5-glia-α3 are indicated.
See this image and copyright information in PMC

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