Blocking celiac antigenicity of the glutamine-rich gliadin 33-mer peptide by microbial transglutaminase
Author:
Affiliation:
1. State Key Laboratory of Food Science and Technology
2. Nanchang University
3. Nanchang 330047
4. China
5. School of Food Science and Technology
6. Nanchang 330031
7. College of Pharmaceutical Sciences
Abstract
Transamidation by mTG with variety of acyl-acceptor substrates decreased the antigenicity of gliadin peptide related to celiac disease.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2017/RA/C6RA27893K
Reference29 articles.
1. The Oslo definitions for coeliac disease and related terms
2. Integration of Genetic and Immunological Insights into a Model of Celiac Disease Pathogenesis
3. Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease
4. HLA-DQ2 and -DQ8 signatures of gluten T cell epitopes in celiac disease
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