Celiac Disease and Immunogenic Wheat Gluten Peptides and the Association of Gliadin Peptides with HLA DQ2 and HLA DQ8

ABSTRACT

Wheat consists mainly of gluten with about 30% gliadin and 50% glutenin, which give gluten its unique viscoelastic properties and also mainly associated with the cause of celiac disease. Although the hydrolysis of gluten has been characterized, the discovery of new gluten-based peptides with high affinity toward T-cells is challenging. Currently, the highly immunogenic 33-mer gliadin peptide is considered to be the main cause of celiac disease. Thus, having consistent data for different gluten peptides with their respective immunogenicity is urgently needed. This report summarizes the various immunogenic gluten peptides identified, and the ingestion of specific gliadin peptide leading to the onset of CD, caused by the immunogenic α/β-gliadins especially in relation to the binding sites on HLA-DQ2 and HLA-DQ8.

KEYWORDS:

• Gluten
• gliadin peptides
• immunogenic peptides
• celiac disease
• wheat allergy
• gluten hydrolysisIntroduction

Author Contributions

Kalekristos Yohannes: writing, reviewing and editing. Juanli Yuan: editing the immunogenic and pathogenic section of the manuscript. Wan Zhen and Qinglin Yu: software and graphic design. Yating Cao: summarization and illustration design for the mechanism of CD, Mao Huijia: manuscript editing and investigation. Hongyan Li: visualization and assisting on submission. Yingli Liu: reviewing, supervision, and validation. Jing Wang: project supervision, administration and funding acquisition. Baoguo Sun: funding acquisition.

Acknowledgments

This work was supported by National Key Research and Development Program of China (No. 2018YFD0401200), Beijing Excellent Talents Funding for Youth Scientist Innovation Team (2016000026833TD01) and High-level Teachers in Beijing Municipal Universities (IDHT20180506).

Conflicts of Interest

No conflict of interest exists in the submission of this manuscript, and it is approved by all authors for publication.

Notes

¹ Data on the tertiary structure is based on the measured radii of gyration (R_g) and radii of gyration of the cross-section (R_c) using 70% (v/v) aqueous ethanol over the concentration range of 1 to 10 mg of protein/mL, and analysis of small-angle X-ray scattering (SAXS) profiles by Guinier analysis and cross-section Guinier approximation.

Additional information

Funding

This work was supported by the Beijing Excellent Talents Funding for Youth Scientist Innovation Team [2016000026833TD01]; National Key Research and Development Program of China [2018YFD0401200]; High-level Teachers in Beijing Municipal Universities [IDHT20180506].