CALL FOR PAPERS Innovative and Emerging Technologies in GI Physiology and Disease Effect of Rothia mucilaginosa enzymes on gliadin (gluten) structure, deamidation, and immunogenic epitopes relevant to celiac disease
نویسندگان
چکیده
Na Tian, Guoxian Wei, Detlef Schuppan, and Eva J. Helmerhorst Department of Molecular and Cell Biology, Henry M. Goldman School of Dental Medicine, Boston, Massachusetts; Division of Gastroenterology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts; and Institute of Translational Immunology and Research Center for Immunology (FZI), University Medical Center, Johannes-Gutenberg-University, Mainz, Germany
منابع مشابه
Identification of food-grade subtilisins as gluten-degrading enzymes to treat celiac disease.
Gluten are proline- and glutamine-rich proteins present in wheat, barley, and rye and contain the immunogenic sequences that drive celiac disease (CD). Rothia mucilaginosa, an oral microbial colonizer, can cleave these gluten epitopes. The aim was to isolate and identify the enzymes and evaluate their potential as novel enzyme therapeutics for CD. The membrane-associated R. mucilaginosa protein...
متن کاملIdentification of Rothia Bacteria as Gluten-Degrading Natural Colonizers of the Upper Gastro-Intestinal Tract
BACKGROUND Gluten proteins, prominent constituents of barley, wheat and rye, cause celiac disease in genetically predisposed subjects. Gluten is notoriously difficult to digest by mammalian proteolytic enzymes and the protease-resistant domains contain multiple immunogenic epitopes. The aim of this study was to identify novel sources of gluten-digesting microbial enzymes from the upper gastro-i...
متن کاملHLA-DQ2 and -DQ8 signatures of gluten T cell epitopes in celiac disease.
Celiac disease is associated with HLA-DQ2 and, to a lesser extent, HLA-DQ8. Type 1 diabetes is associated with the same DQ molecules in the opposite order and with possible involvement of trans-encoded DQ heterodimers. T cells that are reactive with gluten peptides deamidated by transglutaminase 2 and invariably restricted by DQ2 or DQ8 can be isolated from celiac lesions. We used intestinal T ...
متن کاملCeliac disease: antibody recognition against native and selectively deamidated gliadin peptides.
BACKGROUND Selective deamidation of glutamine residues by tissue transglutaminase (tTG) turns gliadin peptides into stronger activators of T cells from celiac disease (CD) patients. We examined the possibility that these modified peptides could be more specific epitopes for circulating antibodies than are native peptides. METHODS Two native synthetic peptides and their respective modified seq...
متن کاملIdentification of immunodominant epitopes of alpha-gliadin in HLA-DQ8 transgenic mice following oral immunization.
Celiac disease, triggered by wheat gliadin and related prolamins from barley and rye, is characterized by a strong association with HLA-DQ2 and HLA-DQ8 genes. Gliadin is a mixture of many proteins that makes difficult the identification of major immunodominant epitopes. To address this issue, we expressed in Escherichia coli a recombinant alpha-gliadin (r-alpha-gliadin) showing the most conserv...
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