Agents for treating celiac disease

Abstract

The invention relates to the field of novel chimeric HLA class II molecules. The invention also relates to the field of novel chimeric HLA class II fusion polypeptides, nucleic acids, vectors, modified cells and compositions directed against celiac disease. Associated methods for use in treating and / or preventing celiac disease are also provided herein.

Description

[0001]Agents for treating Celiac Disease The invention relates to the field of novel chimeric HLA class II molecules, fusion polypeptides, nucleic acids, vectors, modified cells and compositions directed against celiac disease. Associated methods for use in treating or preventing celiac disease are also provided herein. Background Celiac disease (CD), also known as coeliac disease or celiac spruce, is a small intestinal disease caused by a pro-inflammatory T cell response to the food antigen gluten. Celiac disease affects between 0.5 to 2% of the population in Europe, the America’s, the Middle East, Northern Africa, India, China and Australia. At present, the only available treatment for celiac disease is a strict lifelong gluten-free diet which is complicated by the widespread use of gluten in the food industry, wheat being one of the most commonly consumed cereals worldwide. Gluten and the gluten-like proteins hordein and secalin are an integral component of wheat, barley and rye respectively. As such, they are an essential component of commonly consumed foods including but not restricted to bread, pasta, and pizza. In addition, gluten is often added to food products not readily associated with cereals like soy sauce, instant meals and soups. Celiac disease occurs in subjects possessing either HLA-DQ2 and / or HLA-DQ8. HLA- DQ molecules bind to peptides derived from endogenous or exogenous sources and display HLA-DQ:peptide complexes on the surface of antigen presenting cells. If the peptides are derived from a pathogen, HLA-DQ:peptide complexes are recognized by T cell receptors (TCRs) expressed by CD4+ T cells. CD4+ T cells specifically interact with a HLA-DQ:peptide complex, leading to T cell activation and the mounting of an immune response to eradicate the pathogen. HLA-DQ2 and HLA-DQ8 are uniquely suited to bind proline-rich and transglutaminase (TG2) modified gluten-derived peptides. HLA-DQ2 and HLA-DQ8 have a strong preference for negatively charged amino acids at particular positions in the bound peptide that serve to anchor the bound peptide tightly into the peptide-binding groove. While gluten itself does not contain such negatively charged amino acids, negatively charged amino acids are incorporated into gluten peptides in the small intestine to form gluten-derived peptides. When gluten peptides enter the small intestine, the enzyme tissue TG2 converts glutamine residues in the gluten peptides into glutamic acid, thus producing proline-rich and TG2 modified gluten- derived peptides. Due to their strong association, HLA-DQ2 and HLA-DQ8 bind to said proline-rich and TG2 modified gluten-derived peptides, forming HLA-DQ:gluten-derived peptide complexes. CD4+ T cells expressing T cell receptors bind specifically to these HLA-DQ:gluten-derived peptide complexes, resulting in T cell activation and the pro-inflammatory phenotype found in subjects with celiac disease. Gluten is a complex mixture of proteins consisting of gliadins and glutenin, where the gliadins can be subdivided in α-, γ-, and ω-gliadins and the glutenins in the (high molecular weight) HMW-glutenins and low molecular weight (LMW)-glutenins. Although immunogenic peptides can be found in all of these proteins classes, the T cell response in HLA-DQ2 positive celiac disease subjects is directed to peptide sequences in the N-terminal part of α-gliadin and homologous sequences thereof in ω-gliadin. The ω-gliadin sequences are identical to sequences found in the hordeins of barley and the secalins of rye. Similarly, in HLA-DQ8 positive celiac disease subjects, the T cell response is directed to peptide sequences in the C-terminal part of α-gliadin. Therefore, the T cell response in subjects with celiac disease is focussed on α-gliadin, ω-gliadin, hordein and secalin derived peptides. It has been shown that such T cells can persist for decades, providing a likely explanation for the lifelong requirement of a gluten free diet. Accordingly, there is a need for preventing and / or eliminating this T cell response, and thus provide an improved means for treating celiac disease. Summary of the Invention The invention provides a chimeric HLA class II molecule comprising: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain and (ii) a transmembrane domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:3, SEQ ID NO: 4 and SEQ ID NO: 5 (preferably SEQ ID NO: 5) and an HLA-DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:3, SEQ ID NO: 4 and SEQ ID NO: 5 (preferably SEQ ID NO: 5) and an HLA-DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:44, SEQ ID NO: 45 and SEQ ID NO: 46 (preferably SEQ ID NO: 46) and an HLA-DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:44, SEQ ID NO: 45 and SEQ ID NO: 46 (preferably SEQ ID NO: 46) and an HLA-DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:3. SEQ ID NO:4, SEQ ID NO: 5, SEQ ID NO: 44, SEQ ID NO: 45 and SEQ ID NO: 46 (preferably SEQ ID NO: 5 and SEQ ID NO: 46) and an HLA-DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:3. SEQ ID NO:4, SEQ ID NO: 5, SEQ ID NO: 44, SEQ ID NO: 45 and SEQ ID NO: 46 (preferably SEQ ID NO: 5 and SEQ ID NO: 46) and an HLA-DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:3, SEQ ID NO: 4 and SEQ ID NO: 5 (preferably SEQ ID NO: 5) and an HLA-DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively. Optionally, the HLA-DQB1*02 is HLA-DQB1*02:01 and the HLA- DQA1*05 is HLA-DQA1*05:01. See for example SEQ ID NO: 13 and SEQ ID NO: 7. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:3, SEQ ID NO: 4 and SEQ ID NO: 5 (preferably SEQ ID NO: 5) and an HLA-DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively. Optionally, the HLA-DQB1*02 is HLA-DQB1*02:01 and the HLA- DQA1*05 is HLA-DQA1*05:01. See for example SEQ ID NO: 13 and SEQ ID NO: 7. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:44, SEQ ID NO: 45 and SEQ ID NO: 46 (preferably SEQ ID NO: 46) and an HLA-DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively. Optionally, the HLA-DQB1*02 is HLA-DQB1*02:01 and the HLA- DQA1*05 is HLA-DQA1*05:01. See for example SEQ ID NO: 13 and SEQ ID NO: 7. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:44, SEQ ID NO: 45 and SEQ ID NO: 46 (preferably SEQ ID NO: 46) and an HLA-DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively. Optionally, the HLA-DQB1*02 is HLA-DQB1*02:01 and the HLA- DQA1*05 is HLA-DQA1*05:01. See for example SEQ ID NO: 13 and SEQ ID NO: 7. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:3. SEQ ID NO:4, SEQ ID NO: 5, SEQ ID NO: 44, SEQ ID NO: 45 and SEQ ID NO: 46 (preferably SEQ ID NO: 5 and SEQ ID NO: 46) and an HLA-DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively. Optionally, the HLA-DQB1*02 is HLA-DQB1*02:01 and the HLA- DQA1*05 is HLA-DQA1*05:01. See for example SEQ ID NO: 13 and SEQ ID NO: 7. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes selected from SEQ ID NO:3. SEQ ID NO:4, SEQ ID NO: 5, SEQ ID NO: 44, SEQ ID NO: 45 and SEQ ID NO: 46 (preferably SEQ ID NO: 5 and SEQ ID NO: 46) and an HLA-DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively. Optionally, the HLA-DQB1*02 is HLA-DQB1*02:01 and the HLA- DQA1*05 is HLA-DQA1*05:01. See for example SEQ ID NO: 13 and SEQ ID NO: 7. The transmembrane domain may be CD28. The molecule may further comprise a co-stimulatory domain (e.g. CD28) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising a gluten- derived epitope comprising the amino acid sequence of SEQ ID NO: 61 and an HLA-DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. See for example SEQ ID NO: 77 and SEQ ID NO: 76. The transmembrane domain may be CD28 or HLA-DQ. The molecule may further comprise a co- stimulatory domain (e.g. CD28 or 4-1BB) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising a gluten- derived epitope comprising the amino acid sequence of SEQ ID NO: 61 and an HLA- DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. See for example SEQ ID NO: 77 and SEQ ID NO: 76. The transmembrane domain may be CD28 or HLA-DQ. The molecule may further comprise a co- stimulatory domain (e.g. CD28 or 4-1BB) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising a gluten- derived epitope comprising the amino acid sequence of SEQ ID NO: 61 and an HLA- DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. See for example SEQ ID NO: 77 and SEQ ID NO: 76. The transmembrane domain may be CD28 or HLA-DQ. The molecule may further comprise a co- stimulatory domain (e.g. CD28 or 4-1BB) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising a gluten- derived epitope comprising the amino acid sequence of SEQ ID NO: 61 and an HLA- DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. See for example SEQ ID NO: 77 and SEQ ID NO: 76. The transmembrane domain may be CD28 or HLA-DQ. The molecule may further comprise a co- stimulatory domain (e.g. CD28 or 4-1BB) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising a gluten- derived epitope comprising the amino acid sequence of SEQ ID NO: 61 and an HLA- DQ β1β2 chain and (ii) a transmembrane domain (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. See for example SEQ ID NO: 77 and SEQ ID NO: 76. The transmembrane domain may be CD28 or HLA-DQ. The molecule may further comprise a co- stimulatory domain (e.g. CD28 or 4-1BB) and / or a primary signalling domain (e.g. CD3 zeta). Suitably, the chimeric HLA class II molecule may comprise: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising a gluten- derived epitope comprising the amino acid sequence of SEQ ID NO: 61 and an HLA- DQ β1β2 chain (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain and (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. See for example SEQ ID NO: 77 and SEQ ID NO: 76. The transmembrane domain may be CD28 or HLA-DQ. The molecule may further comprise a co- stimulatory domain (e.g. CD28 or 4-1BB) and / or a primary signalling domain (e.g. CD3 zeta). Fusion polypeptides, nucleic acids, vectors, modified cells and compositions directed against celiac disease corresponding to the above are also provided herein. The invention provides a fusion polypeptide, comprising, in an N-terminal to C-terminal orientation: (a) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain; (b) a transmembrane domain; (c) a peptide cleavage signal; (d) a second extracellular domain comprising an HLA-DQ α1α2 chain; (e) a transmembrane domain; wherein the polypeptide further comprises an immune receptor intracellular signalling domain located at the C-terminus of (b) and / or (e), and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. Suitably, the fusion polypeptide may further comprise an HLA-DQ β1β2 chain signal sequence located N-terminal to the first extracellular domain; and an HLA-DQ α1α2 chain signal sequence located N-terminal to the second extracellular domain. Suitably, the one or more gluten-derived epitopes may be from a protein selected from the group consisting of: gliadin, glutenin, hordein, secalin and avenin. Suitably, the gliadin may be alpha gliadin or omega gliadin. Suitably, the gliadin may be alpha gliadin. Suitably, the one or more gluten-derived epitopes may comprise the amino acid sequence of SEQ ID NO: 3, SEQ ID NO: 4, or SEQ ID NO: 69. Suitably, the one or more gluten-derived epitopes may comprise the amino acid sequence of SEQ ID NO: 61. Suitably, the gluten-derived peptide may comprise two or more gluten-derived epitopes. Suitably, the gluten-derived peptide may comprise the amino acid sequences of SEQ ID NO: 3 and SEQ ID NO: 4; or SEQ ID NO: 69 and SEQ ID NO:4. Suitably, the gluten-derived peptide may comprise the amino acid sequence of SEQ ID NO: 5 or SEQ ID NO: 70. Suitably, the gliadin may be omega gliadin. Suitably, the one or more gluten-derived epitopes may comprise the amino acid sequence of SEQ ID NO: 44. Suitably, the one or more gluten-derived epitopes may comprise the amino acid sequence of SEQ ID NO: 45. Suitably, the gluten-derived peptide may comprise the amino acid sequence of SEQ ID NO: 44 and SEQ ID NO: 45. Suitably, the gluten-derived peptide may comprise the amino acid sequence of SEQ ID NO: 46. Suitably, the gluten-derived peptide may comprise four or more gluten-derived epitopes. Suitably, the gluten-derived peptides may be selected from the group consisting of SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO: 69, SEQ ID NO: 44 and SEQ ID NO: 45. Suitably, the gluten-derived peptide may comprise: (a) the amino acid sequence of SEQ ID NO: 5 and SEQ ID NO: 46, optionally wherein the gluten-derived peptide comprises a linker between the amino acid sequence of SEQ ID NO: 5 and SEQ ID NO: 46, or (b) the amino acid sequence of SEQ ID NO: 70 and SEQ ID NO: 46, optionally wherein the gluten-derived peptide comprises a linker between the amino acid sequence of SEQ ID NO: 70 and SEQ ID NO: 46. Suitably, the first extracellular domain may further comprise a linker sequence between the gluten-derived peptide and the HLA-DQ β1β2 chain. Suitably, the gluten-derived peptide may further comprise flanking amino acids at the N- and / or C- terminal side of the gluten-derived epitope, optionally wherein the flanking amino acids are natural flanking amino acids. Suitably, the transmembrane domain may be selected from the group consisting of: alpha or beta chain of CD28, CD4, CD5, CD8, CD9, CD16, CD22, CD27, CD33, CD37, CD45, CD64, CD80, CD86, CD134, CD137, CD152, CD154, PD1, HLA-DR, HLA-DQ or HLA-DP. Suitably, the transmembrane domain may be a CD28 transmembrane domain. Suitably, the transmembrane domain may be a HLA-DQ transmembrane domain. Suitably, the immune receptor intracellular signalling domain may comprise one or more co-stimulatory signalling domains. Suitably, the one or more co-stimulatory signalling domain may be selected from the group consisting of: TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, TLR10, CARD11, CD2, CD7, CD27, CD28, CD30, CD40, CD54 (ICAM), CD83, CD134 (0X40), CD137 (4-1BB), CD154 (CD40L), CD278 (ICOS), DAP10, LAT, NKD2C, SLP76, TRIM, and ZAP70 co-stimulatory signalling domain. Suitably, the one or more co-stimulatory signalling domain may be a CD28 co- stimulatory signalling domain. Suitably, the one or more co-stimulatory signalling domain may be a CD137 co- stimulatory signalling domain. Suitably, the immune receptor intracellular signalling domain may comprise a primary signalling domain. Suitably, the primary signalling domain may be selected from the group consisting of: FcRγ, FcRβ, CD3γ, CD3δ, CD3ε, CD3ζ, CD22, CD79b, and CD66d. Suitably, the primary signalling domain may be CD3ζ. The invention provides a nucleic acid encoding a chimeric HLA class II molecule disclosed herein, or a fusion polypeptide disclosed herein, optionally wherein the nucleic acid is RNA and / or DNA. The invention provides a vector comprising a nucleic acid disclosed herein. The invention provides a cell comprising one or more nucleic acid, vector, chimeric HLA class II molecule, and / or fusion polypeptide disclosed herein. Suitably, the cell may be a T cell, optionally wherein the T cell is selected from the group consisting of a CD8+ T cell, an NK T cell, CD3+ T cell and γδ T cell, or a mixture of any one thereof. Suitably, the cell may be a NK cell or an innate lymphoid cell (ILC). The invention provides a cell comprising at least two of the following: a) a first nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide disclosed herein, wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA- DQA1*05 and HLA-DQB1*02, respectively; b) a second nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide disclosed herein wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA- DQA1*02 and HLA-DQB1*02, respectively; and / or c) a third nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide disclosed herein, wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA- DQA1*03 and HLA-DQB1*03, respectively. Suitably, the HLA-DQA1*02 and HLA-DQB1*02 may be HLA-DQA1*02:01 and HLA- DQB1*02:02 respectively. Suitably, the HLA-DQA1*05 and HLA-DQB1*02 may be HLA-DQA1*05:01 and HLA- DQB1*02:01 respectively. The invention provides a composition comprising a nucleic acid, vector, chimeric HLA class II molecule, fusion polypeptide and / or cell disclosed herein. The invention provides a pharmaceutical composition comprising a nucleic acid, vector, chimeric HLA class II molecule, fusion polypeptide and / or cell disclosed herein. The invention provides a pharmaceutical composition disclosed herein, for use as a medicament. The invention provides a pharmaceutical composition disclosed herein, for use in treating or preventing celiac disease in a HLA-DQ positive subject. Suitably, the subject may be HLA-DQA1*02-HLA-DQB1*02, HLA-DQA1*05-HLA- DQB1*02, and / or a HLA-DQA1*03-DQB1*03 positive. Brief Description of the Figures Embodiments of the invention are further described hereinafter with reference to the accompanying drawings, in which: Figures 1A to B: Different chimeric HLA class II molecule constructs (also referred to as CHAR constructs / CHAR molecules herein). (A) Graphical representation of a CHAR T cell expressing an HLA-DQ2 CHAR molecule, either linked with gliadin peptide or alternative CLIP peptide; (B) Schematic overview of the HLA-DQ2-gluten or HLA-DQ2-CLIP CHAR constructs; the sequences of the specific peptides are linked to the extracellular part of an HLA-DQB1*02:01 molecule coupled to the CD28 costimulatory transmembrane and intracellular signaling domain, and CD3ζ intracellular signaling domain, coupled to P2A, and the extracellular part of an HLA-DQA1*05:01 molecule coupled to the CD28-CD3ζ, followed by IRES allowing for co-expression of NGFR. Figures 2A to D: Gliadin-specific T cell clones produce IFNγ and IL-2 upon HLA- DQ2 CHAR stimulation. (A) IL-2 release by S2 and S16 clones when incubated with K562 cells expressing different HLA-DQ2 CHAR constructs. In Figure A, for K562+DQ2-glia-a CHAR, the left bar is S2 and the right bar is S16; for CD3 / CD28 beads, the left bar is S2, middle bar is S16, and right bar is SV30 (B) and at different effector: target ratios. In Figure B, for each ratio, the left bar is S2 and the right bar is S16 (C) IFNγ release by S2 and S16 clones when incubated with K562 cells expressing different HLA-DQ2 CHAR constructs. In Figure C, for K562+DQ2-glia-a CHAR, the left bar is S2 and the right bar is S16; for CD3 / CD28 beads, the left bar is S2, middle bar is S16, and right bar is SV30 (D) and at different effector: target ratios. In Figure D, for each ratio, the left bar is S2 and the right bar is S16. Figures 3A to C: Specific lysis of gliadin-specific T cell clones after incubation with HLA-DQ2 CHAR T cells. (A) The percentage of specific lysis by HLA-DQ2-glia-α CHAR (circles), HLA-DQ2-CLIP CHAR (squares), or mock (triangles) T cells of glia-α1-specific S2 clone at different effector: target (E: T) ratios shown in two different donors; LRG (A1) and UTT (A2). (B) The percentage of specific lysis by HLA-DQ2-glia-α CHAR (circles), HLA-DQ2- CLIP CHAR (squares), or mock (triangles) T cells of glia- α2-specific S16 clone at different effector: target (E: T) ratios shown in two different donors; LRG (B1) and UTT (B2). (C) The percentage of specific lysis by HLA-DQ2-glia-α CHAR (circles), HLA-DQ2-CLIP CHAR (squares), or mock (triangles) T cells of glia-γ2-specific SV30 clone at different effector: target (E: T) ratios shown in two different donors; LRG (C1) and UTT (C2). Figure 4A to B: Different HLA-DQ8 CHAR sequences. (A) Graphical representation of a CHAR molecule expressing an HLA-DQ8 molecule. (B) Schematic overview of HLA-DQ8 CHAR vector designs with different transmembrane domains (i.e. CD28 or HLA), different costimulatory domains (i.e. CD28 or 4-1BB), and comprising either one or two intracellular costimulatory and signaling domains. All similar domains between the different constructs contain the exact same amino acid sequences. Inserts 1-5 were made in vector pMP71 and combined with NGFR, inserts -5 and -6 are identical, but -6 was inserted in the vector pMP71 no NGFR. Figure 5: Different HLA-DQ8-gliadin-specific T cell clones secrete IFNγ upon stimulation with HLA-DQ8 CHAR-expressing cells. All constructs were recognized by the different HLA-DQ8-gliadin-specific T cell clones (i.e. S13, C1401, B401, T316 and B403), as well as an HLA-DQ8-glutenin-specific T cell clone (i.e. S12), all expressing different TCR alpha and beta chains and derived from different celiac disease patients, as demonstrated by production of IFNγ secretion, shown on the y-axis, by the HLA-DQ8 restricted gliadin-specific clones, shown on the x-axis, after co-incubation overnight at effector: target ratio of 1:5. No production of IFNγ was observed after co-incubation with an HLA-DQ2-gliadin specific T cell clone (i.e. S2). Figure 6A to B: Specific lysis of a broad range of HLA-DQ8-gliadin specific T cell clones upon co-incubation with HLA-DQ8 CD8+ CHAR T cells. (A) CD8+ T cells transduced to express the different HLA-DQ8 CHARs were all able to lyse HLA-DQ8-restricted gliadin- specific CD4+ T cell clones (i.e. S13, B401 and T316) in a specific manner. The percentage of killing is shown as a % of the target only condition and shown in duplicate for each condition. Co-incubation was done overnight, and tested using CHAR T cells from 2 donors (data only shown for one donor) (B) Cytotoxicity towards an even bigger variety of gliadin-specific T cell clones (i.e. L3-12, S13, C1401, B401, T316 and B403), was demonstrated by HLA-DQ8 CHAR (#6) CD8+ T cells. This demonstrates that all variants of HLA-DQ8 CHAR T cells are highly specific and able to lyse a broad variety of gluten-specific cells. Clone S12 and clone S2 are negative control clones recognizing either a peptide derived from glutenin in the context of HLA-DQ8 (S12) or a peptide derived from gliadin-α1 in the context of DQ2 (S2). The patent, scientific and technical literature referred to herein establish knowledge that was available to those skilled in the art at the time of filing. The entire disclosures of the issued patents, published and pending patent applications, and other publications that are cited herein are hereby incorporated by reference to the same extent as if each was specifically and individually indicated to be incorporated by reference. In the case of any inconsistencies, the present disclosure will prevail. Various aspects of the invention are described in further detail below. Definitions “HLA” and “human leukocyte antigen” are herein defined as a genetic fingerprint on human nucleated cells and platelets, composed of proteins that play a critical role in activating the body's immune system to respond to foreign organisms. In humans and other animals, the HLA is also referred to as the “major histocompatibility complex” (MHC). HLA class II is encoded by three different isotypes, HLA-DR, -DQ, and -DP, and presents antigens (typically peptides) from outside a cell to T-lymphocytes. These particular antigens stimulate multiplication of T-helper cells (also called CD4-positive T cells), which in turn stimulate antibody-producing B-cells to produce antibodies to specific antigens and stimulate cytotoxic T cells to lyse infected cells. Natural HLA class II molecules are heterodimers with two homologous chains, the α and β chains. The α chain is made up of an α1 (antigen-binding e.g. gluten-derived peptide binding) domain, an α2 (conserved) domain, and a transmembrane domain. The β chain is made up of a β1 (antigen-binding e.g. gluten-derived peptide binding) domain, a β2 (conserved) domain, and a transmembrane domain. The α and β chains of HLA class II (HLA-II) molecules or proteins are capable of specifically binding (and therefore presenting) a peptide antigen derived from extracellular proteins, including those of extracellular pathogens, on the cell surface. “Chimeric HLA class II molecule” (referred to herein as “the molecule”, or “chimeric HLA antigen receptor”, or “CHAR” herein) refers to an HLA class II molecule which comprises an HLA-DQ α1α2 chain and a HLA-DQ β1β2 chain, wherein the HLA-DQ β1β2 chain is fused to a gluten-derived peptide. Suitably, the gluten-derived peptide may be presented in the HLA groove of the molecule. Suitable gluten-derived peptides are described elsewhere herein. Suitably, the HLA-DQ α1α2 chain and / or the HLA-DQ β1β2 chain of the molecule may be fused to a transmembrane domain and one or more intracellular signalling domains (optionally containing co-stimulatory domain(s)) (see, e.g., Sadelain et al, Cancer Discov., 3(4):388 (2013); see also Harris and Kranz, Trends Pharmacol. Sci., 37(3):220 (2016), and Stone et al, Cancer Immunol. Immunother., 63(11): 1163 (2014)). In the context of the present disclosure, a chimeric HLA class II molecule that presents the peptide fused to the HLA-DQ β1β2 chain may be referred to as a chimeric HLA class II:peptide complex (where the fused peptide is presented in the HLA groove, thus forming an HLA class II:peptide complex). Accordingly, a chimeric HLA class II molecule may also be referred to herein as a chimeric HLA class II:peptide complex (wherein the gluten-derived peptide is presented within the HLA groove generated by the HLA-DQ α1α2 chain and the HLA-DQ β1β2 chain). The term “extracellular domain” refers to polypeptide domain that, when expressed by a cell, is located at the external surface of a cell. The extracellular domains of the invention comprise the extracellular components of HLA class II molecules, for example, the α1α2 chain and / or β1β2 chain of HLA-DQ2 or -DQ8. The extracellular domain may be derived either from a natural, synthetic, semi-synthetic, or recombinant source. As used herein "specifically binds" or "specific for" refers to an association or union of a binding protein (e.g., a chimeric HLA class II molecule and / or TCR receptor) or a binding domain (or fusion protein thereof) to a target molecule with an affinity or Ka(i.e., an equilibrium association constant of a particular binding interaction with units of 1 / M) equal to or greater than 105M-1(which equals the ratio of the on-rate [kon] to the off-rate [koff] for this association reaction), while not significantly associating or uniting with any other molecules or components in a sample. Binding proteins or binding domains (or fusion proteins thereof) may be classified as "high affinity" binding proteins or binding domains (or fusion proteins thereof) or as "low affinity" binding proteins or binding domains (or fusion proteins thereof). "High affinity" binding proteins or binding domains refer to those binding proteins or binding domains having a Ka of at least 107M-1, at least 108M-1, at least 109M-1, at least 1010M-1, at least 1011M-1, at least 1012M-1, or at least 1013M-1. Low affinity" binding proteins or binding domains refer to those binding proteins or binding domains having a Ka of up to 107M-1,up to 106M-1, up to 105M-1. Alternatively, affinity can be defined as an equilibrium dissociation constant (Kd) of a particular binding interaction with units of M (e.g., 10-5M to 10-13M). In certain embodiments, a receptor or binding domain may have "enhanced affinity," which refers to selected or engineered receptors or binding domains with stronger binding to a target antigen than a wild type (or parent) binding domain. For example, enhanced affinity may be due to a Ka (equilibrium association constant) for the target antigen that is higher than the wild type binding domain, due to a Kd (dissociation constant) for the target antigen that is less than that of the wild type binding domain, due to an off-rate (koff) for the target antigen that is less than that of the wild type binding domain, or a combination thereof. The term “gluten-derived peptide” refers to peptides derived from, or encompassed within, one or more gluten proteins. A gluten protein may be selected from the group consisting of gliadin, glutenin, hordein, secalin and avenin (see, for example, Sollid LM, Tye-Din JA, Qiao SW, Anderson RP, Gianfrani C, Koning F. Update 2020: nomenclature and listing of celiac disease-relevant gluten epitopes recognized by CD4+ T cells. Immunogenetics.2019 Nov 18). Tissue transglutaminase (TG2) can modify proteins by transamidation or deamidation of specific glutamine residues. As would be appreciated by a person of skill in the art, in vivo, TG2 causes selective deamidation of gluten, which in turn, causes the generation of a series of proline-rich and TG2 modified gluten-derived peptides that bind to HLA-DQ2 or -DQ8 molecules with high affinity. In the context of the invention, “gluten-derived peptides” may also be referred to as “gluten peptide or deaminated components thereof”, “deaminated gluten peptide”, “TG2 modified gluten peptide” or “proline-rich gluten peptide”. Similarly, the term “gluten-derived epitope” may also be referred to as “gluten epitope or deaminated components thereof”, “deaminated gluten epitope”, “TG2 modified gluten epitope” or “proline-rich gluten epitope”. As used herein, “gliadin” refers to the aqueous alcohol-soluble fraction of gluten, particularly, but not exclusively, gluten derived from wheat, for example Triticum aestivum. A gliadin protein may be selected from the group consisting of alpha (α), beta (β), gamma (γ) and omega (ω) gliadin. As used herein, “glutenin” refers to the aqueous alcohol-insoluble fraction of gluten, particularly but not exclusively, gluten derived from wheat, for example Triticum aestivum. Glutenin may be selected from the group consisting of low and high molecule weight (LMW and HMW) glutenin. As used herein, “hordein” or “barley hordein” refers to gluten derived from barley, Hordein vulgare. Hordein may be selected from the group consisting of B hordein, C hordein and D hordein. As used herein, “secalin” or “rye secalin” refers to gluten derived from rye, Secale cerale. Secalin may be selected from the group consisting of β secalin, γ secalin and ω secalin. As used herein “avenin” refers to gluten derived from oats, Avena sativa. The term “peptide” as used herein refers to a polymer of amino acids. The peptide may be relatively short (i.e. no more than 20 amino acids; e.g. no more than 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, or 8 amino acids). As used herein, “epitope” refers to that portion of an antigen or a peptide that is recognized by the immune system, for example, a T cell receptor or HLA class I or class II, an antibody, a B cell receptor, which portion is sufficient for high affinity binding. As used herein, “transmembrane domain” (TM domain or TMD) refers to a domain that anchors a polypeptide to the plasma membrane of a cell. The TM domain may be derived either from a natural, synthetic, semi-synthetic, or recombinant source. As used herein “immune receptor intracellular signaling domain” is interchangeable with “intracellular signaling domain” or “endodomain”, and refers to the portion of a protein which transduces the effector function signal and that directs the cell to perform a specialized function. While usually the entire intracellular signaling domain can be employed, in many cases it is not necessary to use the entire domain. To the extent that a truncated portion of an intracellular signaling domain is used, such truncated portion may be used in place of the entire domain as long as it transduces the effector function signal. The term intracellular signaling domain is meant to include any truncated portion of the intracellular signaling domain sufficient to transducing effector function signal. As used herein “HLA-DQA1*02-HLA-DQB1*02” is interchangeable with HLA-DQ2 and refers to an HLA molecule encoded by the genes HLA-DQA1*02 and HLA-DQB1*02. More specifically, in HLA-DQ2, the α1α2 chain is encoded by the gene HLA-DQA1*02 and the β1β2 chain is encoded by HLA-DQB1*02. Suitably, the HLA-DQ2 molecule may be an HLA-DQ2.5 or HLA-DQ2.2 molecule. A HLA-DQ2.5 molecule comprises an α1α2 chain encoded by the gene HLA- DQA1*05:01 and a β1β2 chain encoded by the gene HLA-DQB1*02:01. Herein, the HLA- DQ2.5 molecule may also be referred to as “HLA-DQA1*05:01-HLA-DQB1*02:01”. Accordingly, a subject that is HLA-DQ2.5 positive is a subject that comprises HLA-DQ2.5, and may be referred to herein as an “HLA-DQA1*05:01-HLA-DQB1*02:01” positive subject. An HLA-DQ2.2 molecule comprises an α1α2 chain encoded by the gene HLA- DQA1*02:01 and a β1β2 chain encoded by the gene HLA-DQB1*02:02. Herein, the HLA- DQ2.2 molecule may also be referred to as “HLA-DQA1*02:01-HLA-DQB1*02:02”. Accordingly, a subject that is HLA-DQ2.2 positive is a subject that comprises HLA-DQ2.2, and may be referred to herein as an “HLA-DQA1*02:01-HLA-DQB1*02:02” positive subject. An HLA-DQ8 molecule comprises an α1α2 chain encoded by the gene HLA- DQA1*03 and a β1β2 chain encoded by the gene HLA-DQB1*03. Suitably the HLA-DQA1*03 gene encoding the α1α2 chain may be HLA-DQA1*03:01 or HLA-DQA1*03:02. Suitably the HLA-DQB1*03 gene encoding the β1β2 chain may be HLA-DQB1*03:02. Herein, the HLA- DQ8 molecule may also be referred to as “HLA-DQA1*03:01-HLA-DQB1*03” or “HLA- DQA1*03:02-HLA-DQB1*03”. Accordingly, a subject that is HLA-DQ8 positive is a subject that comprises HLA-DQ8, and may be referred to herein as an “HLA-DQA1*03-HLA-DQB1*03 positive” subject. As used herein, “fusion polypeptide” refers to one or more polypeptide domains or segments. Fusion polypeptides are typically linked N-terminus to C-terminus, although they can also be linked C-terminus to C-terminus, N-terminus to N- terminus, or C-terminus to N- terminus. In particular embodiments, the polypeptides of the fusion protein can be in any order. Fusion polypeptides or fusion proteins can also include conservatively modified variants, polymorphic variants, alleles, mutants, subsequences, and interspecies homologs, so long as the desired activity of the fusion polypeptide is preserved. Fusion polypeptides may be produced by chemical synthetic methods or by chemical linkage between the two moieties or may generally be prepared using other standard techniques. As used herein, “peptide cleavage signal” is interchangeable with “polypeptide cleavage site” and “protease cleavage sites”, and refers to a polypeptide cleavage signal between each of the polypeptide domains described herein. In addition, a polypeptide cleavage site can be put into any linker peptide sequence. Exemplary polypeptide cleavage signals include polypeptide cleavage recognition sites such as protease cleavage sites, nuclease cleavage sites (e.g., rare restriction enzyme recognition sites, self-cleaving ribozyme recognition sites), and self-cleaving viral oligopeptides (see deFelipe and Ryan, 2004. Traffic, 5(8); 616-26). As used herein, “linker sequence” is interchangeable with “linker” and refers to a plurality of amino acid residues between the various polypeptide domains added for appropriate spacing and conformation of the molecule. As used herein, “immunodominant” refers to a peptide stimulating immune responses to a greater extent than other peptides. As used herein, “flanking amino acids” is interchangeable with “flanking sequences” and refers to amino acid residues adjacent to a specific amino acid sequence of interest. In the context of the present disclosure, the specific amino acid sequence of interest may be the gluten-derived peptide. Accordingly, the flanking amino acids may be those adjacent to the gluten-derived peptide. The flanking amino acids may be adjacent to the N- or C-terminal of the peptide. By being “adjacent” as used herein means abutting or in close proximity to the amino acid sequence of interest (for example no more than 1 or 2 amino acid residues away from the amino acid sequence of interest. More suitably, the flanking amino acid abuts the amino acid sequence of interest. Merely by way of example, the flanking amino acid may be 1, 2, 3, 4, or 5 amino acids in length. More suitably, the flanking amino acid may be 1 or 2 amino acids in length. As used herein, the term, “co-stimulatory signaling domain,” or “co-stimulatory domain” refers to an intracellular signaling domain of a co-stimulatory molecule. Co- stimulatory molecules are cell surface molecules other than antigen receptors or Fc receptors that provide a second signal required for efficient activation and function of T lymphocytes upon binding to antigen. As used herein “primary signaling domain” refers to an intracellular signaling domain that regulates the primary activation of the chimeric HLA class II molecule either in a stimulatory way, or in an inhibitory way. Primary signaling domains that act in a stimulatory manner may contain signaling motifs which are known as immunoreceptor tyrosine-based activation motifs or ITAMs. As used herein “nucleic acid sequence”, “polynucleotide”, “nucleic acid” and “nucleic acid molecule” are used interchangeably to refer to an oligonucleotide sequence or polynucleotide sequence. The nucleotide sequence may be of genomic, synthetic or recombinant origin, and may be double-stranded or single-stranded (representing the sense or antisense strand). The term "nucleotide sequence" includes genomic DNA, cDNA, synthetic DNA, and RNA (e.g. mRNA) and analogs of the DNA or RNA generated, e.g., by the use of nucleotide analogs. As used herein, “isolated nucleic acid sequence” or “isolated nucleic acid composition” refers to a nucleic acid sequence that is not in its natural environment when it is linked to its naturally associated sequence(s) that is / are also in its / their natural environment. In other words, an isolated nucleic acid sequence / composition is not a native nucleotide sequence / composition, wherein "native nucleotide sequence / composition" means an entire nucleotide sequence that is in its native environment and when operatively linked to an entire promoter with which it is naturally associated, which promoter is also in its native environment. Such a nucleic acid could be part of a vector and / or such nucleic acid or polypeptide could be part of a composition (e.g., a cell lysate), and still be isolated in that such vector or composition is not part of the natural environment for the nucleic acid or polypeptide. The term "gene" means the segment of DNA involved in producing a polypeptide chain; it includes regions preceding and following the coding region ("leader and trailer") as well as intervening sequences (introns) between individual coding segments (exons). The nucleic acid sequences of the invention may be a non-naturally occurring nucleic acid sequence (e.g. it may be that the entire sequence does not occur in its entirety in nature). For example, the nucleic acid sequence of the invention may be operably linked to a promoter, wherein the promoter is not naturally associated with equivalent human nucleic acid sequences in nature (e.g. HLA sequences or fragments thereof); i.e. it is not the entire promoter that is naturally associated with the nucleic acid in its natural environment. In this context, such promoters may be considered exogenous promoters. In some examples, a protein and a gene encoding said protein may be referred to using the same term (e.g. HLA-DQ2). In examples where a protein and a gene encoding said protein are referred to using the same term (e.g. HLA-DQ2 etc), a person of skill in the art would readily be able to determine whether the protein or the gene was being referred to depending on the context in which the term was mentioned. As used herein, the term “vector” refers to a nucleic acid sequence capable of transporting another nucleic acid sequence to which it has been operably linked. The vector can be capable of autonomous replication or it can integrate into a host DNA. The vector may include restriction enzyme sites for insertion of recombinant DNA and may include one or more selectable markers or suicide genes. The vector can be a nucleic acid sequence in the form of a plasmid, a bacteriophage or a cosmid. As used herein, the term "cell" is interchangeable with “host cell” or “modified cell” and includes any cell into which the nucleic acid, vector, CHAR, fusion polypeptide described herein may be introduced. Once a nucleic acid, vector, CHAR, fusion polypeptide has been introduced into the cell, it may be referred to as a “modified cell” herein. Once the nucleic acid, vector, CHAR, fusion polypeptide is introduced into the host cell, the resultant modified cell should be capable of expressing the encoded binding protein (and e.g. correctly localising the encoded binding protein for its intended function e.g. transporting the encoded binding protein to the cell surface). As used herein, a pharmaceutical composition may comprise a nucleic acid, vector, CHAR or fusion polypeptide described herein along with a pharmaceutically acceptable excipient, adjuvant, diluent and / or carrier. As used herein, "pharmaceutically acceptable" refers to a material that is not biologically or otherwise undesirable, i.e., the material may be administered to an individual along with the selected nucleic acid, vector, CHAR or fusion polypeptide without causing any undesirable biological effects or interacting in a deleterious manner with any of the other components of the pharmaceutical composition in which it is contained. Pharmaceutically acceptable excipients are well known in the art. A suitable excipient is therefore easily identifiable by one of ordinary skill in the art. By way of example, suitable pharmaceutically acceptable excipients include water, saline, aqueous dextrose, glycerol, ethanol, and the like. As used herein, the terms “treat”, “treating” and "treatment" are taken to include an intervention performed with the intention of preventing the development or altering the pathology of a condition, disorder or symptom (e.g. celiac disease or a celiac disease related condition). Accordingly, "treatment" refers to both therapeutic treatment and prophylactic or preventative measures, wherein the object is to prevent or slow down (lessen) the targeted condition, disorder or symptom. “Treatment” therefore encompasses a reduction, slowing or inhibition of the amount or concentration of target cells, for example as measured in a sample obtained from the subject, of at least 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or 100% when compared to the amount or concentration of target cells before treatment. Methods of measuring the amount or concentration of target cells include, for example, qRT- PCR, and quantification of disease specific biomarkers in a sample obtained from the subject. As used herein the term “subject” refers to an individual, e.g., a human, having or at risk of having a specified condition, disorder or symptom. The subject may be a patient i.e. a subject in need of treatment in accordance with the invention. The subject may have received treatment for the condition, disorder or symptom. Alternatively, the subject has not been treated prior to treatment in accordance with the present invention. As used herein, the term “HLA-DQ positive” refers to a subject who possess either HLA-DQ2 or HLA-DQ8. Such individuals mount an inappropriate HLA-DQ2- and / or DQ8- restricted CD4+ T cell-mediated immune response to gluten-derived peptides. Detailed Description The present invention provides a chimeric HLA class II molecule comprising: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and a HLA-DQ β1β2 chain and (ii) a transmembrane domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising a HLA-DQ α1α2 chain (ii) a transmembrane domain and wherein the first and / or second polypeptide further comprises an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. In one embodiment, the chimeric HLA class II molecule comprises: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain (ii) a transmembrane domain; and (iii) an immune receptor intracellular signalling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain (ii) a transmembrane domain; and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. In one embodiment, the chimeric HLA class II molecule comprises: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain; (ii) a transmembrane domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain (ii) a transmembrane domain; and (iii) an immune receptor intracellular signalling domain; and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. In one embodiment, the chimeric HLA class II molecule comprises: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain (ii) a transmembrane domain; and (iii) an immune receptor intracellular signalling domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain (ii) a transmembrane domain; and (iii) an immune receptor intracellular signalling domain; and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. The inventors surprisingly discovered that a chimeric HLA class II molecule according to the invention is able to treat and / or prevent celiac disease. Tissue transglutaminase (TG2) is a crucial factor in celiac disease because it promotes gluten-specific T cell responses. In vivo, TG2 causes selective deamidation of gluten, which in turn, causes the generation of a series of proline-rich and TG2 modified gluten-derived peptides that bind to HLA-DQ2 or -DQ8 molecules with high affinity. Responses to these peptides are detectable in all patients with CD. In particular the T cell response in HLA-DQ2.5 positive CD patients is focussed on 2 overlapping 9 amino acid peptide sequences in the N- terminal part of the α-gliadins (e.g. (i) HLA-DQ2-glia-α1a: PFPQPELPY (SEQ ID NO:3) and HLA-DQ2-glia-α2: PQPELPYPQ (SEQ ID NO: 4), which are both present in the 11-mer sequence PFPQPELPYPQ, (SEQ ID NO: 5); or (ii) HLA-DQ2-glia-α1b: PYPQPELPY (SEQ ID NO:69) and HLA-DQ2-glia-α2: PQPELPYPQ (SEQ ID NO: 4), which are both present in the 11-mer sequence PYPQPELPYPQ, (SEQ ID NO: 70)), and homologous sequences thereof in the ω-gliadins (PFPQPEQPF (SEQ ID NO: 44) and PQPEQPFPW (SEQ ID NO: 45), combined PFPQPEQPFPW (SEQ ID NO: 46)). Of note, the latter ω-gliadin sequences are identical to sequences found in the hordeins of barley and the secalins of rye, providing an explanation for the shared toxicity of wheat, barley and rye for patients with CD. Similarly, in HLA-DQ8 positive patients the response is directed to an immunodominant peptide sequence from the C-terminal part of the α-gliadins (EGSFQPSQE, SEQ ID NO: 61). In one embodiment, the one or more gluten-derived epitopes are from the protein gliadin. Suitably, the gliadin may be alpha gliadin. Suitably, the one or more alpha gliadin-derived epitope may be glia-α, for example glia-α1 or glia-α2. Suitably, the one or more alpha gliadin-derived epitope may be glia-α1, for example glia- α1 or glia-α2. In one embodiment, the one or more alpha gliadin-derived epitope comprises the amino acid sequence of SEQ ID NO: 3. SEQ ID NO: 3 corresponds to the peptide HLA- DQ2-glia-α1a. HLA-DQ2-glia-α1a is an immunodominant peptide of celiac disease. Therefore, it is advantageous for a cell (such as a CD8+ T cell) to express a CHAR according to the invention (which presents the immunodominant peptide HLA-DQ2-glia-α1a) because it has the ability to be effective at killing a key population of CD4+ T cells responsible for causing CD. In one embodiment, the one or more alpha gliadin-derived epitope comprises the amino acid sequence of SEQ ID NO: 69. SEQ ID NO: 69 corresponds to the peptide HLA-DQ2-glia- α1b. HLA-DQ2-glia-α1b is an immunodominant peptide of celiac disease. Therefore, it is advantageous for a cell (such as a CD8+ T cell) to express a CHAR according to the invention (which presents the immunodominant peptide HLA-DQ2-glia-α1b) because it has the ability to be effective at killing a key population of CD4+ T cells responsible for causing CD. Suitably, the one or more alpha gliadin-derived epitope may be glia-α2. In one embodiment, the one or more alpha gliadin-derived epitope comprises the amino acid sequence of SEQ ID NO: 4. SEQ ID NO:4 encodes HLA-DQ2-glia-α2. HLA-DQ2-glia-α2 is also an immunodominant peptide of celiac disease. Therefore, it is advantageous for a cell (such as a CD8+ T cell) to express a CHAR according to the invention (which presents the immunodominant peptide HLA-DQ2-glia-α2) because it has the ability to be effective at killing a key population of CD4+ T cells responsible for causing CD. In one embodiment, the gluten-derived peptide comprises two or more alpha gliadin- derived epitopes. In a preferred embodiment, the gluten-derived peptide comprises the amino acid sequences of SEQ ID NO: 3 and SEQ ID NO: 4. As it would be appreciated a cell (such as a CD8+ T cell) that expresses such a chimeric HLA class II molecule would be capable of forming two distinct HLA:peptide complexes, each targeting and eliminating a distinct CD4+ T cell population that is responsible causing CD. In one embodiment, the gluten-derived peptide comprises two or more alpha gliadin- derived epitopes. In a preferred embodiment, the gluten-derived peptide comprises the amino acid sequences of SEQ ID NO: 69 and SEQ ID NO: 4. As it would be appreciated a cell (such as a CD8+ T cell) that expresses such a chimeric HLA class II molecule would be capable of forming two distinct HLA:peptide complexes, each targeting and eliminating a distinct CD4+ T cell population that is responsible causing CD. In one embodiment, the gluten-derived peptide comprises the amino acid sequence of SEQ ID NO: 5. The immunodominant HLA-DQ2-glia-α1a and HLA-DQ2-glia-α2 are both contained within the 11-mer sequence PFPQPELPYPQ (SEQ ID NO:5). Surprisingly, and advantageously, a cell (such as a CD8+ T cell) expressing a CHAR comprising and therefore presenting the 11-mer sequence PFPQPELPYPQ has the ability to target distinct CD4+ T cell populations, directed towards either HLA-DQ2-glia-α1a or HLA-DQ2-glia-α2, simultaneously. In one embodiment, the gluten-derived peptide comprises the amino acid sequence of SEQ ID NO: 70. The immunodominant HLA-DQ2-glia-α1b and HLA-DQ2-glia-α2 are both contained within the 11-mer sequence PYPQPELPYPQ (SEQ ID NO:70). Surprisingly, and advantageously, a cell (such as a CD8+ T cell) expressing a CHAR comprising and therefore presenting the 11-mer sequence PyPQPELPYPQ has the ability to target distinct CD4+ T cell populations, directed towards either HLA-DQ2-glia-α1b or HLA-DQ2-glia-α2, simultaneously. In one embodiment, the one or more alpha gliadin-derived epitope comprises the amino acid sequence of SEQ ID NO: 61. SEQ ID NO: 61 corresponds to the peptide HLA-DQ8-glia- α1. Therefore, it is advantageous for a cell (e.g. a CD8+ T cell) to express a CHAR according to the invention (which presents the immunodominant peptide HLA-DQ8-glia-α1) because it has the ability to be effective at killing a key population of CD4+ T cells responsible for causing CD. In one embodiment, the gluten-derived peptide comprises two or more alpha gliadin- derived epitopes. In a preferred embodiment, the gluten-derived peptide comprises the amino acid sequences of SEQ ID NO: 61 and one or more of SEQ ID NO: 3, SEQ ID NO: 4, and / or SEQ ID NO: 5. As it would be appreciated a cell (e.g. a CD8+ T cell) that expresses such a chimeric HLA class II molecule would be capable of forming two distinct peptide:HLA complexes, each targeting and eliminating a distinct CD4+ T cell population that is responsible causing CD. In one embodiment, the gluten-derived peptide comprises two or more alpha gliadin- derived epitopes. In a preferred embodiment, the gluten-derived peptide comprises the amino acid sequences of SEQ ID NO: 61 and one or more of SEQ ID NO: 69, SEQ ID NO: 4, and / or SEQ ID NO: 70. As it would be appreciated a cell (e.g. a CD8+ T cell) that expresses such a chimeric HLA class II molecule would be capable of forming two distinct peptide:HLA complexes, each targeting and eliminating a distinct CD4+ T cell population that is responsible causing CD. In one embodiment, the gliadin is omega gliadin. In one embodiment, the one or more omega gliadin-derived epitope comprises the amino acid sequence of SEQ ID NO: 44. SEQ ID NO: 44 encodes HLA-DQ2-glia-Ω1. HLA-DQ2-glia-Ω1 is another immunodominant peptide of celiac disease. Therefore, it is advantageous for a cell (e.g. a CD8+ T cell) to express a CHAR according to the invention (which presents the immunodominant peptide HLA-DQ2- glia-Ω1) because it has the ability to be effective at killing a key population of CD4+ T cells responsible for causing CD. In one embodiment, the one or more omega gliadin-derived epitope comprises the amino acid sequence of SEQ ID NO: 45. SEQ ID NO:45 encodes HLA-DQ2-glia-Ω2. HLA-DQ2-glia- Ω2 is an also an immunodominant peptide of celiac disease. Therefore, it is advantageous for a cell (e.g. a CD8+ T cell) to express a CHAR according to the invention (which presents the immunodominant peptide HLA-DQ2-glia-Ω2) because it has the ability to be effective at killing a key population of CD4+ T cells responsible for causing CD. In one embodiment, the gluten-derived peptide comprises two or more omega gliadin- derived epitopes. In a preferred embodiment, the gluten-derived peptide comprises the amino acid sequences of SEQ ID NO: 44 and SEQ ID NO: 45. As it would be appreciated a cell (e.g. a CD8+ T cell) that expresses such a chimeric HLA class II molecule would be capable of forming a two distinct peptide:HLA complexes, each targeting and eliminating a distinct CD4+ T cell population that is responsible causing CD. In one embodiment, the gluten-derived peptide comprises the amino acid sequence of SEQ ID NO: 46. The immunodominant HLA-DQ2-glia-Ω1 and HLA-DQ2-glia-Ω2 are both contained within the 11-mer sequence (SEQ ID NO: 46). Surprisingly, and advantageously, a cell (such as a CD8+ T cell) expressing a CHAR comprising and therefore presenting the 11- mer sequence PFPQPEQPFPW has the ability to target distinct CD4+ T cell populations, directed towards either HLA-DQ2-glia-Ω1 or HLA-DQ2-glia-Ω2, simultaneously. In one embodiment, the gluten-derived peptide comprises two or more gluten-derived epitopes, e.g. gliadin-derived epitopes. Suitably, in an embodiment that comprises two or more gluten-derived epitopes, at least one of the epitopes may be an alpha gliadin-derived epitope, and / or at least one of the epitopes may be an omega gliadin-derived epitope. In one embodiment, the two or more gluten-derived epitopes may be selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 44, SEQ ID NO: 45, and SEQ ID NO: 46. Suitably, when the gluten-derived peptide comprises two or more gluten-derived epitopes, one epitope may be according to SEQ ID NO: 5, and one may be according to SEQ ID NO: 46. Suitably, when the gluten-derived peptide comprises two or more gluten-derived epitopes, one epitope may be according to SEQ ID NO: 70, and one may be according to SEQ ID NO: 46. Advantageously, such a CHAR comprising two or more distinct gluten-derived epitopes is able to target and eliminate two or more distinct CD4+ T cell populations that are responsible for CD. In one embodiment, the gluten-derived peptide comprises four or more gluten-derived epitopes, e.g. gliadin-derived epitopes. Suitably, in an embodiment that comprises four or more gluten-derived epitopes, at least one of the epitopes may be an alpha gliadin-derived epitope, and / or at least one of the epitopes may be an omega gliadin-derived epitope. In one embodiment, the four or more gluten-derived epitopes may be selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 44, SEQ ID NO: 45, and SEQ ID NO: 46. Suitably, when the gluten-derived peptide comprises four or more gluten-derived epitopes, the four or more may be SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 44, and SEQ ID NO: 45. Suitably, when the gluten-derived peptide comprises four or more gluten-derived epitopes, the four or more may be SEQ ID NO: 69, SEQ ID NO: 4, SEQ ID NO: 44, and SEQ ID NO: 45. Advantageously, such a CHAR comprising two or more distinct gluten-derived epitopes is able to target and eliminate four or more distinct CD4+ T cell populations that are responsible for CD. In some embodiments, wherein the gluten-derived peptide comprises two or more gluten- derived epitopes, the gluten-derived peptide comprises a linker separating the amino acid sequences of the epitopes. In some embodiments, the first extracellular domain further comprises a linker sequence between the gluten-derived peptide and the HLA-DQ β1β2 chain. An example of a suitable linker is provided as SEQ ID NO: 6. Peptides that are longer than the conventional 9mer sequence presented by HLA may be used within the chimeric HLA class II molecule or fusion polypeptide provided herein. For example, the gluten-derived peptides described herein may be from 9 to 35 amino acids long. For the avoidance of doubt, in this context, the peptides can have a total of 9 to 35 amino acids, which includes the one or more gluten-derived epitope. The additional amino acids may be located N-terminal or C-terminal to the one or more gluten-derived epitope sequence. Alternatively, the additional amino acids may flank the one or more gluten-derived epitope sequence (i.e. such that there are additional amino acid(s) N-terminal and C-terminal of the one or more gluten-derived epitope sequence). Additional amino acids located N-terminal, C- terminal or flanking the one or more gluten-derived epitope are referred to collectively as “flanking amino acids” herein. The N-terminus of a peptide (also known as the amino-terminus, N-terminus, N-terminal end or amine-terminus) is the start of a peptide terminated by an amino acid with a free amine group (-NH2). By convention, peptide sequences are written N-terminus to C-terminus (from left to right). The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C- terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). As used herein, the terms “N-terminal” and “C-terminal” are used to describe the relative position of e.g. a sequence within a peptide or polypeptide. Accordingly, a sequence that is “N-terminal” is positioned closer (in relative terms) to the N-terminus than to the C-terminus of the peptide or polypeptide. Conversely, a domain that is “C-terminal” is positioned (in relative terms) closer to the C- terminus than to the N-terminus of the peptide or polypeptide. As used herein, the term “positioned” refers to the location of the sequence within the linear amino acid sequence of the peptide or polypeptide. Where the peptides described herein include additional amino acids located N- terminal, C-terminal or flanking the one or more gluten-derived epitopes, any appropriate additional amino acid sequences may be included. For example, the additional amino acids may be amino acid sequences that are naturally located N-terminal, C-terminal or flanking the gluten- derived epitope sequence. In a particular example, the additional amino acids are located at N- terminal to the one or more gluten-derived epitope sequence and may be the natural sequence that is found N- terminal to the one or more gluten-derived epitope. In another example, the additional amino acids may be all be located C-terminal to the one or more gluten-derived epitope sequence and may be the natural sequence that is found C-terminal to the one or more gluten-derived epitope sequence. Alternatively, the additional amino acids may flank the one or more gluten-derived epitope sequence (i.e. such that there are additional amino acid(s) N-terminal and C-terminal of the one or more gluten-derived epitope sequence) and may be the natural sequence that flank the one or more gluten-derived epitope sequence. Advantageously, flanking amino acids mimic natural peptide:HLA complex formation, resulting in higher binding affinity between the peptide:HLA complex and CD4 T cells. In one example, when the gluten-derived peptide comprises the gluten-derived epitope of SEQ ID NO: 5, the gluten-derived peptide may comprise an N-terminal flanking sequence of QLQ and / or a C-terminal flacking region of PQL. In other words, the gluten-derived peptide may comprise the sequence QLQPFPQPELPYPQ (SEQ ID NO: 63), QLQPFPQPELPYPQPQL (SEQ ID NO: 64) or PFPQPELPYPQPQL (SEQ ID NO: 65). In one example, when the gluten-derived peptide comprises the gluten-derived epitope of SEQ ID NO: 46, the gluten-derived peptide may comprise an N-terminal flanking sequence of PQQ and / or a C-terminal flacking region of QPQ. In other words, the gluten-derived peptide may comprise the sequence PQQPFPQPEQPFPW (SEQ ID NO: 66), PQQPFPQPEQPFPWQPQ (SEQ ID NO: 67) or PFPQPEQPFPWQPQ (SEQ ID NO: 68). In one example, when the gluten-derived peptide comprises the gluten-derived epitope of SEQ ID NO: 70, the gluten-derived peptide may comprise an N-terminal flanking sequence of QLQ and / or a C-terminal flacking region of PQL. In other words, the gluten-derived peptide may comprise the sequence QLQPYPQPELPYPQ (SEQ ID NO: 71), QLQPYPQPELPYPQPQL (SEQ ID NO: 72) or PYPQPELPYPQPQL (SEQ ID NO: 73). The invention also provides a fusion polypeptide, comprising, in an N-terminal to C- terminal orientation: (a) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain; (b) a transmembrane domain; (c) a peptide cleavage signal; (d) a second extracellular domain comprising an HLA-DQ α1α2 chain; (e) a transmembrane domain; wherein the polypeptide further comprises an immune receptor intracellular signalling domain located at the C-terminus of (b) and / or (e), and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*03 and HLA-DQB1*03, respectively. For avoidance of doubt the fusion polypeptide described herein may form a chimeric HLA class II molecule as described herein. For example, the fusion polypeptide may be cleaved at the peptide cleavage signal to form a first polypeptide (comprising an α1α2 chain) and a second polypeptide (comprising a β1β2 chain), wherein the first and second polypeptide together form a chimeric HLA class II molecule of the invention. Several fusion polypeptides are described herein, see for example SEQ ID NO: 1, SEQ ID NO: 43, SEQ ID NO: 55, SEQ ID NO: 74, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO: 83 and SEQ ID NO:84 which are described in the examples section below). As will be appreciated, embodiments described in relation to the chimeric HLA class II molecule of the invention apply equally to the fusion polypeptide of the invention unless the context specifically indicates otherwise. In one embodiment the fusion polypeptide comprises in an N-terminal to C-terminal orientation: (a) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain; (b1) a transmembrane domain; (b2) an immune receptor intracellular signalling domain (c) a peptide cleavage signal; (d) a second extracellular domain comprising an HLA-DQ α1α2 chain; (e) a transmembrane domain; and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*03 and HLA-DQB1*03, respectively. In another embodiment the fusion polypeptide comprises in an N-terminal to C-terminal orientation: (a) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain; (b) a transmembrane domain; (c) a peptide cleavage signal; (d) a second extracellular domain comprising an HLA-DQ α1α2 chain; (e1) a transmembrane domain; (e2) an immune receptor intracellular signalling domain; and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*03 and HLA-DQB1*03, respectively. In another embodiment the fusion polypeptide comprises in an N-terminal to C-terminal orientation: (a) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain; (b1) a transmembrane domain; (b2) an immune receptor intracellular signalling domain (c) a peptide cleavage signal; (d) a second extracellular domain comprising an HLA-DQ α1α2 chain; (e1) a transmembrane domain; (e2) an immune receptor intracellular signalling domain; and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*03 and HLA-DQB1*03, respectively. In one embodiment, the fusion polypeptide may further comprise a linker sequence between the immune receptor intracellular signalling domain and the peptide cleavage signal. In one embodiment, the polypeptide cleavage signal is a viral self-cleaving polypeptide. In a preferred embodiment, the peptide cleavage signal is a viral self-cleaving 2A polypeptide (see for example SEQ ID NO: 11). Other exemplary protease cleavage sites include, but are not limited to, the cleavage sites of potyvirus Ma proteases (e.g., tobacco etch virus protease), potyvirus HC proteases, potyvirus P1 (P35) proteases, byovirus Ma proteases, byovirus RNA- 2-encoded proteases, aphthovirus L proteases, enterovirus 2A proteases, rhinovirus 2A proteases, picorna 3C proteases, comovirus 24K proteases, nepovirus 24K proteases, RTSV (rice tungro spherical virus) 3C-like protease, PYVF (parsnip yellow fleck virus) 3C-like protease, heparin, thrombin, factor Xa and enterokinase. In one embodiment, the polypeptide cleavage signal may be an internal ribosome entry site (IRES) sequence. In one embodiment, the fusion polypeptide may further comprise an internal ribosome entry site (IRES) after the transmembrane domain that is C-terminal to the α1α2 chain. In another embodiment, the fusion polypeptide further comprises a IRES and truncated nerve growth factor receptor (NGFR) at the C-terminus of the fusion polypeptide (in an N- to C- terminal orientation). As described herein, the chimeric HLA class II molecule and the fusion polypeptide of the invention comprise HLA-DQ α1α2 and β1β2 chains. As would be clear to a person of skill in the art, the HLA-DQ α1α2 and β1β2 chains within a chimeric HLA class II molecule or fusion polypeptide must be capable of forming a heterodimeric HLA class II complex. In a suitable embodiment, the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*05 and HLA-DQB1*02, respectively; or the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*02 and HLA-DQB1*02, respectively; or the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*03 and HLA-DQB1*03, respectively. In an embodiment when the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*02 and HLA-DQB1*02, HLA-DQA1*02 may be HLA-DQA1*0201 or HLA- DQA1*0202. In an embodiment when the HLA-DQ α1α2 and β1β2 chains are encoded by the gene HLA-DQA1*03 and HLA-DQB1*03, HLA-DQA1*03 may be HLA-DQA1*0301 or HLA- DQA1*0302, and optionally HLA-DQB1*03 may be HLA-DQB1*0302. As described elsewhere herein, the chimeric HLA class II molecule or the fusion polypeptide of the invention comprise a transmembrane domain. In one embodiment, the transmembrane domain is selected from the group consisting of: alpha or beta chain of CD28, CD4, CD5, CD8, CD9, CD16, CD22, CD27, CD33, CD37, CD45, CD64, CD80, CD86, CD134, CD137, CD152, CD154, PD1, HLA-DR, HLA-DQ or HLA-DP. In a specific embodiment, the transmembrane domain is a CD28 transmembrane domain (see for example, SEQ ID NO:8). Suitably, the transmembrane domain is a HLA-DQ transmembrane domain. As described elsewhere herein, the chimeric HLA class II molecule or the fusion polypeptide of the invention comprise a immune receptor intracellular signalling domain. In one embodiment, the immune receptor intracellular signalling domain comprises one or more co-stimulatory signalling domains. In a specific embodiment, the one or more co-stimulatory signalling domain is selected from the group consisting of: TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, TLR10, CARD11, CD2, CD7, CD27, CD28, CD30, CD40, CD54 (ICAM), CD83, CD134 (0X40), CD137 (4-1BB), CD154 (CD40L), CD278 (ICOS), DAP10, LAT, NKD2C, SLP76, TRIM, and ZAP70 co-stimulatory signalling domain. For example, the one or more co-stimulatory signalling domain may be a CD28 co-stimulatory signalling domain (see for example SEQ ID NO: 9). Suitably, the one or more co-stimulatory signalling domain may be a CD137 (4-1BB) co-stimulatory signalling domain. Suitably, the one or more co- stimulatory domains may comprise a CD28 co-stimulatory signalling domain and a CD137 co- stimulatory domain. The immune receptor intracellular signalling domain may (further) comprise a primary signalling domain. In one embodiment, the primary signalling domain may be selected from the group consisting of: FcRγ, FcRβ, CD3γ, CD3δ, CD3ε, CD3ζ, CD22, CD79b, and CD66d. In a specific embodiment, the primary signalling domain is CD3ζ (see for example, SEQ ID NO: 10). In one embodiment, the chimeric HLA class II molecule or the fusion polypeptide of the invention may comprise one or more immune receptor signalling domains, e.g. one or more co-stimulatory signalling domains and / or one or more primary signalling domains. The invention provides a nucleic acid encoding a chimeric HLA class II molecule according to the invention, or a fusion polypeptide according to the invention. Suitably, the nucleic acid may be DNA or RNA, or a combination thereof. The invention provides a vector comprising said nucleic acid. Any appropriate vector can be used. By way of example only, the vector may be a plasmid, a cosmid, or a viral vector, such as a retroviral vector or a lentiviral vector. Adenovirus, adeno-associated virus, vaccinia virus, canary poxvirus, herpes virus, minicircle vectors and naked (synthetic) DNA / RNA may also be used (for details on minicircle vectors, see for example non-viral Sleeping Beauty transposition from minicircle vectors as published by R Monjezi et al., Leukemia 2017). Alternatively, single stranded or double stranded DNA or RNA can be used to transfect lymphocytes with a TCR of interest (see Roth et al 2018 Nature vol 559; page 405). In one example, the vector is a plasmid, a viral vector, or a cosmid, optionally wherein the vector is selected from the group consisting of a retrovirus, lentivirus, adeno-associated virus, adenovirus, vaccinia virus, canary poxvirus, herpes virus, minicircle vector and synthetic DNA or RNA. Preferably the (expression) vector is capable of propagation in a host cell and is stably transmitted to future generations. The vector may comprise regulatory sequences. "Regulatory sequences" as used herein, refers to, DNA or RNA elements that are capable of controlling gene expression. Examples of expression control sequences include promoters, enhancers, silencers, TATA- boxes, internal ribosomal entry sites (IRES), attachment sites for transcription factors, transcriptional terminators, polyadenylation sites etc. Optionally, the vector includes one or more regulatory sequences operatively linked to the nucleic acid sequence to be expressed. Regulatory sequences include those which direct constitutive expression, as well as tissue- specific regulatory and / or inducible sequences. Optionally, the vector comprises the nucleic acid sequence of interest operably linked to a promoter. "Promoter", as used herein, refers to the nucleotide sequences in DNA to which RNA polymerase binds to start transcription. The promoter may be inducible or constitutively expressed. Alternatively, the promoter is under the control of a repressor or stimulatory protein. The promoter may be one that is not naturally found in the host cell (e.g. it may be an exogenous promoter). The skilled person in the art is well aware of appropriate promoters for use in the expression of target proteins, wherein the selected promoter will depend on the host cell. "Operably linked" refers to a single or a combination of the below-described control elements together with a coding sequence in a functional relationship with one another, for example, in a linked relationship so as to direct expression of the coding sequence. The vector may comprise a transcriptional terminator. “Transcriptional terminator” as used herein, refers to a DNA element, which terminates the function of RNA polymerases responsible for transcribing DNA into RNA. Preferred transcriptional terminators are characterized by a run of T residues preceded by a GC rich dyad symmetrical region. The vector may comprise a translational control element. “Translational control element”, as used herein, refers to DNA or RNA elements that control the translation of mRNA. Preferred translational control elements are ribosome binding sites. Preferably, the translational control element is from a homologous system as the promoter, for example a promoter and its associated ribozyme binding site. Preferred ribosome binding sites are known, and will depend on the chosen host cell. The vector may comprise restriction enzyme recognition sites. "Restriction enzyme recognition site" as used herein, refers to a motif on the DNA recognized by a restriction enzyme. Preferably the vector comprises those genetic elements which are necessary for expression of the binding proteins described herein by a host cell. The elements required for transcription and translation in the host cell include a promoter, a coding region for the protein(s) of interest, and a transcriptional terminator. A person of skill in the art will be well aware of the molecular techniques available for the preparation of (expression) vectors and how the (expression) vectors may be transduced or transfected into an appropriate host cell (thereby generating a modified cell described further below). The (expression) vector system described herein can be introduced into cells by conventional techniques such as transformation, transfection or transduction. “Transformation”, “transfection” and “transduction” refer generally to techniques for introducing foreign (exogenous) nucleic acid sequences into a host cell, and therefore encompass methods such as electroporation, microinjection, gene gun delivery, transduction with retroviral, lentiviral or adeno-associated vectors, lipofection, superfection etc. The specific method used typically depends on both the type of vector and the cell. Appropriate methods for introducing nucleic acid sequences and vectors into host cells such as human cells are well known in the art; see for example Sambrook et al (1989) Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; Ausubel et al (1987) Current Protocols in Molecular Biology, John Wiley and Sons, Inc., NY; Cohen et al (1972) Proc. Natl. Acad. Sci. USA 69, 2110; Luchansky et al (1988) Mol. Microbiol. 2, 637-646. Further conventional methods that are suitable for preparing expression vectors and introducing them into appropriate host cells are described in detail in WO2016 / 071758 for example. The invention provides a cell comprising one or more nucleic acid, vector, chimeric HLA class II molecule, and / or fusion polypeptide according to the invention. The invention also provides a cell comprising at least two of the following: a) a first nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide according to any one of the preceding claims, wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; b) a second nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide according to any one of the preceding claims, wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; and / or c) a third nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide according to any one of the preceding claims, wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively. Such a cell is advantageous as it is capable of simultaneously targeting distinct T cell populations that recognise distinct HLA-DQ2:peptide and / or HLA-DQ8:peptide complexes. In one example, the cell of the invention may encode two CHARs separated by a linker (e.g. one that encodes HLA-DQ2 and PFPQPELPYPQ; linked to another that encodes HLA- DQ8 and EGSFQPSQE) such that at least two distinct CHARs are expressed on the same T cell (each one targeting a different TCR repertoire). This would be useful in patients that are both HLA-DQ2 positive (95% of patients) and HLA-DQ8 positive, as the resultant CHAR CD8+ T cell would be able to target TCRs that recognise: HLA-DQ2:PFPQPELPY complexes; HLA- DQ2:PQPELPYPQ complexes and HLA-DQ8:EGSFQPSQE complexes. In one example, the cell of the invention may encode two CHARs separated by a linker (e.g. one that encodes HLA-DQ2 and PYPQPELPYPQ; linked to another that encodes HLA- DQ8 and EGSFQPSQE) such that at least two distinct CHARs are expressed on the same T cell (each one targeting a different TCR repertoire). This would be useful in patients that are both HLA-DQ2 positive (95% of patients) and HLA-DQ8 positive, as the resultant CHAR CD8+ T cell would be able to target TCRs that recognise: HLA-DQ2:PYPQPELPY complexes; HLA- DQ2:PQPELPYPQ complexes and HLA-DQ8:EGSFQPSQE complexes. In one example, the cell of the invention may encode two CHARs separated by a linker (e.g. one that encodes HLA-DQ2 and PFPQPEQPFPW; linked to another that encodes HLA- DQ8 and EGSFQPSQE) such that at least two distinct CHARs are expressed on the same T cell (each one targeting a different TCR repertoire). This would be useful in patients that are both HLA-DQ2 positive (95% of patients) and HLA-DQ8 positive, as the resultant CHAR CD8+ T cell would be able to target TCRs that recognise: HLA-DQ2: PFPQPEQPF complexes; HLA- DQ2: PQPEQPFPW complexes and HLA-DQ8:EGSFQPSQE complexes. The cell is typically a eukaryotic cell, and particularly a human cell. Suitably, the cell may be a human immune cell, for example a T cell, NK cell, or an innate lymphoid cell (ILC). Suitably, the T cell may be selected from the group consisting of CD8+T cell, CD3+ T cell, NK T cell, and gamma delta T cell (γδ T cell), or a mixture of any one thereof. Suitably, the cell is a CD8+T cell. Suitably, the cell is a CD3+ T cell. The cell may be an autologous or allogeneic cell. “Allogeneic cell” refers to a cell derived from a different individual to the individual to which it is later administered. In other words, the cell may be an isolated cell from a distinct individual compared to the subject to be treated. “Autologous cell” refers to a cell derived from the individual to which it is also later administered. In other words, the cell may be an isolated cell from the subject that is to be treated. The invention provides a composition comprising a nucleic acid, vector chimeric HLA class II molecule, fusion polypeptide and / or cell according to the invention. The invention provides a pharmaceutical composition comprising a nucleic acid, vector, chimeric HLA class II molecule, fusion polypeptide and / or cell according to the invention. Suitably, said pharmaceutical composition is for use as a medicament. The invention provides a pharmaceutical composition comprising a nucleic acid, vector, chimeric HLA class II molecule, fusion polypeptide and / or cell according to the invention for use in treating or preventing celiac disease in an HLA-DQ positive subject. CHAR, fusion polypeptides, compositions, nucleic acid molecule, or cells of the invention may advantageously be used to treat or prevent celiac disease in a subject. An appropriate composition may be selected independently of the HLA serotype of the subject. In the alternative, an appropriate composition may be selected on the basis of the HLA-DQ serotype and / or HLA-DR serotype of the subject. Suitably, the subject is HLA-DQA1*02-HLA-DQB1*02, HLA-DQA1*05-HLA- DQB1*02, and / or HLA-DQA1*03-DQB1*03 positive. Throughout the description and claims of this specification, the words “comprise” and “contain” and variations of them mean “including but not limited to”, and they are not intended to (and do not) exclude other moieties, additives, components, integers or steps. Throughout the description and claims of this specification, the singular encompasses the plural unless the context otherwise requires. In particular, where the indefinite article is used, the specification is to be understood as contemplating plurality as well as singularity, unless the context requires otherwise. Features, integers, characteristics, compounds, chemical moieties or groups described in conjunction with a particular aspect, embodiment or example of the invention are to be understood to be applicable to any other aspect, embodiment or example described herein unless incompatible therewith. Various aspects of the invention are described in further detail below. Unless defined otherwise herein, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains. Although any methods and materials similar or equivalent to those described herein find use in the practice of the present invention, the preferred methods and materials are described herein. Accordingly, the terms defined immediately below are more fully described by reference to the Specification as a whole. Also, as used herein, the singular terms "a", "an," and "the" include the plural reference unless the context clearly indicates otherwise. Unless otherwise indicated, nucleic acids are written left to right in 5' to 3' orientation; amino acid sequences are written left to right in amino to carboxy orientation, respectively. It is to be understood that this invention is not limited to the particular methodology, protocols, and reagents described, as these may vary, depending upon the context they are used by those of skill in the art. Aspects of the invention are demonstrated by the following non-limiting examples. Examples The inventors have investigated whether cytotoxic CD8 T cells expressing HLA-DQ2 coupled to a costimulatory signalling and CD3ζ signalling domain and loaded with the relevant immunodominant α- and ω-gliadin peptides would be able to specifically interact with gliadin- specific T cells from patients, resulting in the elimination of these disease-causative CD4 T cells. To obtain proof of concept they generated the chimeric HLA class II molecule constructs (also referred to as chimeric HLA antigen receptor (CHAR) constructs) shown in Figure 1. The inventors identified that the immunodominant HLA-DQ2-glia-α1a and HLA-DQ2- glia-α2 are both contained within the 11-mer sequence PFPQPELPYPQ. They reasoned that if the 11-mer sequence PFPQPELPYPQ was encoded within the HLA-DQ2 beta construct both the HLA-DQ2-glia-α1a and HLA-DQ2-glia-α2 epitope would be expressed by the CHAR T cells, allowing the ability to target CD4 T cells directed towards both HLA-DQ2-glia-α1a and HLA-DQ2-glia-α2 simultaneously with a single CAR T cell. As a control, HLA-DQ2 constructs containing the alternative CLIP peptide were also generated. Cells were transduced with the HLA-DQ2 CHAR constructs by using retroviral transduction. Expression of the HLA-DQ2 CHAR construct was first confirmed on K562 cells using different human monoclonal antibodies specific for HLA-DQ2. K562 cells expressing the HLA-DQ CHAR constructs were then enriched and used as stimulator cells to confirm that the DQ-glia-α1a and DQ-glia-α2 epitopes were presented in HLA-DQ2 on the cell surface. This was investigated using a panel of CD patient-derived T cell clones described previously. In short, those T cell clones were derived from small intestinal biopsies obtained from CD patients undergoing endoscopy for diagnostic purposes. Their (fine)specificity was determined by testing against synthetic variants of gluten-derived peptides, TCR sequences were determined where appropriate, and structural studies underpinned the observed specificity. The inventors tested three T cell clones, one specific for the HLA-DQ2-glia-α1a epitope (S2), one specific for the HLA-DQ2-glia-α2 epitope (S16), and one specific for the unrelated HLA-DQ2-glia-γ2 epitope (SV30). To determine the conformation and integrity of the HLA- DQ2 CHAR construct, the three T cell clones (specific for each of S2, S16 and SV30) were incubated with CHAR construct transduced K562 cells and it was tested whether the T cell clones recognized the CHAR construct. The inventors observed IL-2 and IFNγ production when the HLA-DQ2-glia-α1a and HLA-DQ2-glia-α2 specific T cell clones were incubated with K562 cells transduced with gluten-derived peptide-linked HLA-DQ2 CHAR construct, but not when incubated with K562 cells transduced with CLIP peptide -linked HLA-DQ2 CHAR construct. Moreover, the T cell clone recognizing the unrelated HLA-DQ2-glia-γ2 epitope did not respond to K562 cells transduced with either CHAR constructs confirming the correct conformation and integrity of the HLA-DQ2- α1a and DQ-glia-α2 epitope in the HLA-DQ2 CHAR construct (Figure 2). With the cell surface expression, correct conformation, and integrity of the HLA-DQ2 CHAR construct shown, the ability of CD8+ HLA-DQ2 CHAR T cells to specifically lyse gluten- specific T cell clones was determined (Figure 3). For this purpose, CD8+ T cells were transduced with the HLA-DQ2 CHAR constructs. To investigate if the generated CHAR T cells have the capacity to specifically eliminate T cells specific for the HLA-DQ2-glia-α1a and HLA- DQ2-glia-α2 epitopes, CD patient-derived T cell clones S2 (glia- α1), S16 (glia-α2) and SV30 (glia-γ2) were used. Next, the CD8 T cells of two different healthy donors transduced with either DQ2-glia-α CHAR (SEQ ID NO:1), DQ2-CLIP CHAR, or mock were incubated for 6 hours with 51Cr labelled T cell clones (S2, S16 or SV30). As demonstrated in Figure 3, the DQ2 glia-α CHAR T cells of both donors have the capacity to specifically eliminate CD4 T cells specific for the HLA-DQ2-glia-α1a (S2) and HLA-DQ2-glia-α2 epitope (S16), in a dose- dependent manner, whereas the control T cell clone (SV30) was not killed, demonstrating that a single CHAR T cell can eliminate patient-derived T cells specific for the immunodominant HLA-DQ2-glia-α1a and HLA-DQ2-glia-α2 epitopes simultaneously. Construction design and retroviral production Retroviral vectors encoding CHAR molecules included the signal peptide, followed by the sequence of the overlapping gliadin-alpha-1 and gliadin-alpha-2 peptides (CCGTTTCCGCAGCCGGAACTGCCGTACCCGCAG – SEQ ID NO:31) with additional flanking amino acids, which was connected via a linker to the extracellular part of an HLA- DQB1*02:01 coupled to the transmembrane and intracellular region of CD28, and intracellular signaling domains of CD3ζ, coupled to P2A allowing splicing. Subsequently, the extracellular HLA-DQA1*05:01 molecule is followed by the CD28 transmembrane and intracellular region, as well as the CD3ζ intracellular signaling domains. This is coupled with an internal ribosome entry site (IRES) that permits co-expression of truncated nerve growth factor receptor (NGFR). For the purpose of control, a CHAR construct was engineered with the sequence of the alternative CLIP peptide (CCGCTGCTGATGCAGGCGCTGCCGATG – SEQ ID NO:62) with additional flanking amino acids, instead of the gliadin-alpha peptide. Alternatively, a vector containing only NGFR was used as a mock. Phoenix-AMPHO (ATCC, CRL-3213) or Phoenix- GALV [1] were transiently transfected with various constructs using Fugene HD Transfection Reagent (Promega). The retroviral supernatants were collected and stored at −80°C after 48 hours. Generation of CHAR-expressing cells 24-well flat-bottom culture plates (Greiner Bio-One) were coated with 30 µg / mL of retronectin (Takara) and then blocked with 2% HSA (Sanquin) prior to retroviral transduction. Retroviral supernatants were added and centrifuged at 3000 g for 20 minutes at 4°C. Following the removal of the retroviral supernatant, the cells were transferred to the virus-coated wells. After an overnight incubation, the cells were transferred to 24-well flat-bottom plates (Costar). Seven days after being stimulated by irradiated autologous feeders at 35 Gy and supplemented with phytohaemagglutinin (PHA, Oxoid Microbiology Products, Thermo Fisher Scientific), the transduced cells were MACS enriched for the NGFR gene marker using an NGFR-APC antibody (Sanbio, clone ME20.4), and anti-APC MicroBeads (Milteny, clone BW135 / 80). Human CD8 T-cell isolation and cell culture HLA-DQB1*02:01 / HLA-DQA1*05:01 (HLA-DQ2.5) negative healthy donors were selected from the biobank belonging to the Department of Hematology at Leiden University Medical Center (HEM 008 / SH / sh). PBMCs were isolated through standard Ficoll Isopaque separation and preserved through cryopreservation. PBMCs were thawed and enriched for CD8+ T cells through positive selection using CD8 Microbeads (Miltenyi). CD8+ T cells were stimulated using autologous feeder cells irradiated at 35 Gy and supplemented with phytohaemagglutinin (PHA, Oxoid Microbiology Products, Thermo Fisher Scientific). T cells were cultured in T cell medium (TCM) consisting of IMDM (Gibco) with 5% heat-inactivated FBS (Lonza), 5% heat-inactivated human serum (ABOS, Sanquin), 100 U / mL penicillin, 100 µg / mL streptavidin, 2.7mM L-glutamine (Lonza), and 100 IU / mL IL-2 (Chiron). Gluten-specific T cell culture Gluten-specific CD4+ T-cell clones S2 and S16 recognize DQ2.5-glia-α1a and DQ2.5- glia-α2 respectively [2]. As it recognizes DQ2.5-γ2, SV30 was used as a control [3]. The T-cell clones were thawed and stimulated using allogeneic feeder cells irradiated at 35 Gy, supplemented with PHA and cultured in TCM. Cell lines and cell culture K562 (ATCC, CCL-243™) cells were cultured in IMDM with the addition of 10% heat- inactivated FBS, 100 U / mL penicillin, 100 µg / mL streptavidin, 2.7mM L-glutamine (all from Lonza). All cell lines were regularly tested for mycoplasma contamination. Flow cytometry Cells were washed in PBS supplemented with 1% human serum albumin (HSA) and stained with fluorochrome-conjugated antibodies at 4°C for 20-30 minutes using standard flow cytometry protocols. The CD8 isolated fractions were assessed for purity with PE-labelled CD8β (Beckman Coulter, clone 2ST8.5H7) and FITC-coupled CD4 (BD / Pharmingen, clone RPA- T4). The cell surface expression of CHAR molecules was quantified with human monoclonal antibodies specific for HLA-DQB*02:01 (LB_DQB0201_A, LB_DQB0201_B, and LB_DQB0201_C), and specific for HLA-DQB*03:03 (LB_DQB0303_A) and secondary PE- conjugated goat-anti-human IgG (Jackson, clone 109-116-098). APC-conjugated NGFR (Sanbio, clone ME20.4) was utilized to establish the transduction efficiency and purity of CHAR-transduced cells. Cells were washed and fixed in 1% paraformaldehyde before acquisition using either LSRII or Fortessa flow cytometer instruments (BD) and were analyzed using FlowJo software (Tree star). Appropriate controls were included to authenticate antibody specificity. For the HLA-specific staining, K562 and CD8 CHAR cells were gated on NGFR+. IFNγ and IL2 ELISA IL2 and IFNγ secretion levels were quantified through ELISA using the Invitrogen and Diaclone kits respectively. To quantify cytokine production, supernatants were collected following overnight cocultures of CD4 T cell clones and K562 CHAR-transduced cells and diluted to 1:5 and 1:125. High-binding plates were coated with IFNγ coating antibody overnight to measure IFNγ secretion. The plates were then blocked with 10% bovine serum albumin (BSA) for 2 hours at room temperature. Afterward, supernatant and biotinylated detection antibodies were added for 2 hours at room temperature. Then, streptavidin labeled HRP was added for 30 minutes at room temperature. Finally, a substrate containing 6 mg / mL Tetramethylbenzidine (TMB), and 3% H2O2 was added. Finally, the reaction was halted with the addition of 2M H2SO4. For the production of IL2 by the CD4+ T cell clones, high-binding plates were coated with an IL2 capture antibody overnight. The plates were subsequently blocked with an ELISA / ELISPOT diluent for 1 hour at room temperature. Next, the supernatant was then added for 2 hours at room temperature, followed by the addition of an IL2 detection antibody for 1 hour at room temperature. Then, avidin labeled with HRP was added for 30 minutes at room temperature. Finally, the above-mentioned TMB solution was added, and the reaction was terminated with 2M H2SO4. The absorbance was measured at 450 nm using a microplate reader (Thermo Electron) for both ELISAs. Chromium release assay Cytotoxicity was determined through the use of 51-chromium (51Cr) release assays. CD4+ T cell clones were labeled with 100 µCi 51Cr for one hour at 37 °C. After washing, the cells were cocultured in triplicate with DQ2-glia CHAR, DQ2-CLIP CHAR, or mock transduced T cells at various E: T ratios (ranging from 9:1 to 0,3:1). Spontaneous 51Cr release of the target cells was measured in culture medium alone, and maximum 51Cr release was determined by the addition of 1% Triton-X100 (Sigma-Aldrich). Supernatants were collected after six hours and then transferred onto Lumaplates (Perkin Elmer). The quantity of released 51Cr was measured on a Microbeta counter (Perkin Elmer). The percentage of specific lysis was calculated using the formula ((experimental 51Cr release – average spontaneous 51Cr release) / (average maximal 51Cr release – average spontaneous 51Cr release)) x 100. Additionally, CD8 HLA-DQ8-gliadin CHAR constructs were designed to target a broader repertoire of gluten-specific T cells present in HLA-DQ-positive celiac disease patients. Various retroviral vectors were generated for HLA-DQ8 CHARs comprising different transmembrane domains (i.e. CD28 or HLA), different costimulatory domains (i.e. CD28 or 4- 1BB), and comprising either one or two intracellular costimulatory and signaling domains (Figure 4). These retroviral constructs encoding for the different HLA-DQ8 CHAR molecules were introduced into K562 cells and results demonstrated that similar to HLA-DQ2 CHAR T cells, the HLA- DQ8 CHAR molecules were recognized by a wide variety of previously identified and verified HLA-DQ8-gliadin-specific CD4+ T cell clones derived from celiac disease patient material. This is demonstrated by production of cytokines (IFNγ) by the CD4+ T cell clones upon recognition of the specific peptide / HLA complex (Figure 5). Finally, the inventors demonstrated that CD8 T cells expressing the various HLA-DQ8-gliadin CHARs were able to effectively lyse the HLA-DQ8 gluten-specific CD4+ T cell clones (Figure 6A, B). The reader's attention is directed to all papers and documents which are filed concurrently with or previous to this specification in connection with this application and which are open to public inspection with this specification, and the contents of all such papers and documents are incorporated herein by reference. All of the features disclosed in this specification (including any accompanying claims, abstract and drawings), and / or all of the steps of any method or process so disclosed, may be combined in any combination, except combinations where at least some of such features and / or steps are mutually exclusive. Each feature disclosed in this specification (including any accompanying claims, abstract and drawings), may be replaced by alternative features serving the same, equivalent, or similar purpose, unless expressly stated otherwise. Thus, unless expressly stated otherwise, each feature disclosed is one example only of a generic series of equivalent or similar features. The invention is not restricted to the details of any foregoing embodiments. The invention extends to any novel one, or any novel combination, of the features disclosed in this specification (including any accompanying claims, abstract and drawings), or to any novel one, or any novel combination, of the steps of any method or process so disclosed. SEQUENCES Table 1 : CHAR HLA-DQ2.5-glia-α1a-glia-α2 molecule SEQ ID CHAR Amino Acid (AA), Length Sequence NO POLYPEPTIDE Nucleotide (NT) or Nucleotide Codon Optimised (NT OPT) CHAR_HLA- AA 867 MSWKKALRIPGGLRAATVTLMLSMLSTPVAEGQLQP DQ2.5-glia- FPQPELPYPQPQLGSGSGSLGSGSGSGSGSRDSPEDF α1a-glia-α2 VYQFKGMCYFTNGTERVRLVSRSIYNREEIVRFDSDVG molecule (α- EFRAVTLLGLPAAEYWNSQKDILERKRAAVDRVCRHN gliadin) YQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSVTD FYPAQIKVRWFRNDQEETAGVVSTPLIRNGDWTFQIL VMLEMTPQRGDVYTCHVEHPSLQSPITVEWRAQSES AQSKFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRL LHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRSRV KFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKR RGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEI GMKGERRRGKGHDGLYQGLSTATKDTYDALHMQAL PPRGSGATNFSLLKQAGDVEENPGPMILNKALMLGAL ALTTVMSPCGGEDIVADHVASYGVNLYQSYGPSGQYT HEFDGDEQFYVDLGRKETVWCLPVLRQFRFDPQFALT NIAVLKHNLNSLIKRSNSTAATNEVPEVTVFSKSPVTLG QPNILICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLS KSDHSFFKISYLTLLPSAEESYDCKVEHWGLDKPLLKH WEPEIPAPMSELTETVVCFWVLVVVGGVLACYSLLVT VAFIIFWVRSKRSRLLHSDYMNMTPRRPGPTRKHYQP YAPPRDFAAYRSRVKFSRSADAPAYQQGQNQLYNEL NLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYN ELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTA TKDTYDALHMQALPPR* Signal AA 32 MSWKKALRIPGGLRAATVTLMLSMLSTPVAEG peptide HLA- DQB1*02:01 5' Flanking AA 3 QLQ sequence HLA-DQ2- AA 9 PFPQPELPY glia-α1a HLA-DQ2- AA 9 PQPELPYPQ glia-α2 Complete AA 11 PFPQPELPYPQ alpha gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) 3'Flanking AA 3 PQL sequence Linker AA 17 GSGSGSLGSGSGSGSGS HLA- AA 198 RDSPEDFVYQFKGMCYFTNGTERVRLVSRSIYNREEIV DQB1*02:01 RFDSDVGEFRAVTLLGLPAAEYWNSQKDILERKRAAV DRVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNHHN LLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTPLIRNG DWTFQILVMLEMTPQRGDVYTCHVEHPSLQSPITVE WRAQSESAQSK CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW CD28 co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD primary KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY signaling SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQ domainALPPRLinker AA 3 GSG viral self- AA 19 ATNFSLLKQAGDVEENPGP cleaving 2A polypeptide Signal AA 23 MILNKALMLGALALTTVMSPCGG peptide HLA- DQA1*05:01 HLA- AA 197 EDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYV DQA1*05:01 DLGRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNSL IKRSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNIF PPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLT LLPSAEESYDCKVEHWGLDKPLLKHWEPEIPAPMSELT ETVVC CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW CD28 co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD primary KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY signaling SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQ domain ALPPR Stop AA 1 * CHAR_HLA- NT WT 2601 ATGTCTTGGAAAAAGGCTTTGCGGATCCCCGGAGG DQ2.5-glia- CCTTCGGGCAGCAACTGTGACCTTGATGCTGTCGAT α1a-glia-α2 GCTGAGCACCCCAGTGGCTGAGGGCCAACTTCAAC molecule (α- CTTTTCCTCAACCTGAACTTCCTTATCCTCAACCTCAA gliadin) CTTGGCTCTGGATCTGGGTCCCTGGGATCTGGCTCT GGATCTGGCTCTGGATCTAGAGACTCTCCCGAGGAT TTCGTGTACCAGTTTAAGGGCATGTGCTACTTCACC AACGGGACAGAGCGCGTGCGTCTTGTGAGCAGAAG CATCTATAACCGAGAAGAGATCGTGCGCTTCGACAG CGACGTGGGGGAGTTCCGGGCGGTGACGCTGCTG GGGCTGCCTGCCGCCGAGTACTGGAACAGCCAGAA GGACATCCTGGAGAGGAAACGGGCGGCGGTGGAC AGGGTGTGCAGACACAACTACCAGTTGGAGCTCCG CACGACCTTGCAGCGGCGAGTGGAGCCCACAGTGA CCATCTCCCCATCCAGGACAGAGGCCCTCAACCACC ACAACCTGCTGGTCTGCTCGGTGACAGATTTCTATC CAGCCCAGATCAAAGTCCGGTGGTTTCGGAATGACC AGGAGGAGACAGCTGGCGTTGTGTCCACCCCCCTTA TTAGGAATGGTGACTGGACCTTCCAGATCCTGGTGA TGCTGGAAATGACTCCCCAGCGTGGAGACGTCTACA CCTGCCACGTGGAGCACCCCAGCCTCCAGAGCCCCA TCACCGTGGAGTGGCGGGCTCAATCTGAATCTGCCC AGAGCAAGTTTTGGGTGCTGGTGGTGGTTGGGGGA GTCCTGGCTTGCTATAGCTTGCTAGTAACAGTGGCC TTTATTATTTTCTGGGTGAGGAGTAAGAGGAGCAG GCTCCTGCACAGTGACTACATGAACATGACTCCCCG CCGCCCCGGGCCCACCCGCAAGCATTACCAGCCCTA TGCCCCACCACGCGACTTCGCAGCCTATCGCTCCAG AGTGAAGTTCAGCAGGAGCGCAGACGCCCCCGCGT ACCAGCAGGGCCAGAACCAGCTCTATAACGAGCTC AATCTAGGACGAAGAGAGGAGTACGATGTTTTGGA CAAGAGACGTGGCCGGGACCCTGAGATGGGGGGA AAGCCGAGAAGGAAGAACCCTCAGGAAGGCCTGTA CAATGAACTGCAGAAAGATAAGATGGCGGAGGCCT ACAGTGAGATTGGGATGAAAGGCGAGCGCCGGAG GGGCAAGGGGCACGATGGCCTTTACCAGGGTCTCA GTACAGCCACCAAGGACACCTACGACGCCCTTCACA TGCAGGCCCTGCCCCCTCGCGGCAGCGGCGCCACC AACTTCAGCCTGCTGAAGCAGGCCGGCGACGTGGA GGAAAACCCTGGGCCCATGATCCTAAACAAAGCTCT GATGCTGGGGGCCCTTGCCCTGACCACCGTGATGA GCCCCTGTGGAGGTGAAGACATTGTGGCTGACCAC GTCGCCTCTTATGGTGTAAACTTGTACCAGTCTTACG GTCCCTCTGGCCAGTACACCCATGAATTTGATGGAG ATGAGCAGTTCTACGTGGACCTGGGGAGGAAGGAG ACTGTCTGGTGTTTGCCTGTTCTCAGACAATTTAGAT TTGACCCGCAATTTGCACTGACAAACATCGCTGTCCT AAAACATAACTTGAACAGTCTGATTAAACGCTCCAA CTCTACCGCTGCTACCAATGAGGTTCCTGAGGTCAC AGTGTTTTCCAAGTCTCCCGTGACACTGGGTCAGCC CAACATCCTCATCTGTCTTGTGGACAACATCTTTCCT CCTGTGGTCAACATCACATGGCTGAGCAATGGGCAC TCAGTCACAGAAGGTGTTTCTGAGACCAGCTTCCTC TCCAAGAGTGATCATTCCTTCTTCAAGATCAGTTACC TCACCCTCCTCCCTTCTGCTGAGGAGAGTTATGACT GCAAGGTGGAGCACTGGGGCCTGGACAAGCCTCTT CTGAAACACTGGGAGCCTGAGATTCCAGCCCCTATG TCAGAGCTCACAGAGACTGTGGTCTGCTTTTGGGTG CTGGTGGTGGTTGGGGGAGTCCTGGCTTGCTATAG CTTGCTAGTAACAGTGGCCTTTATTATTTTCTGGGTG AGGAGTAAGAGGAGCAGGCTCCTGCACAGTGACTA CATGAACATGACTCCCCGCCGCCCCGGGCCCACCCG CAAGCATTACCAGCCCTATGCCCCACCACGCGACTT CGCAGCCTATCGCTCCAGAGTGAAGTTCAGCAGGA GCGCAGACGCCCCCGCGTACCAGCAGGGCCAGAAC CAGCTCTATAACGAGCTCAATCTAGGACGAAGAGA GGAGTACGATGTTTTGGACAAGAGACGTGGCCGGG ACCCTGAGATGGGGGGAAAGCCGAGAAGGAAGAA CCCTCAGGAAGGCCTGTACAATGAACTGCAGAAAG ATAAGATGGCGGAGGCCTACAGTGAGATTGGGATG AAAGGCGAGCGCCGGAGGGGCAAGGGGCACGATG GCCTTTACCAGGGTCTCAGTACAGCCACCAAGGACA CCTACGACGCCCTTCACATGCAGGCCCTGCCCCCTC GCTGA Signal NT WT 96 ATGTCTTGGAAAAAGGCTTTGCGGATCCCCGGAGG peptide HLA- CCTTCGGGCAGCAACTGTGACCTTGATGCTGTCGAT DQB1*02:01 GCTGAGCACCCCAGTGGCTGAGGGC 5' Flanking NT WT 9 CAACTTCAA sequence HLA-DQ2- NT WT 26 CCTTTTCCTCAACCTGAACTTCCTTA glia-α1a HLA-DQ2- NT WT 27 CCTCAACCTGAACTTCCTTATCCTCAA glia-α2 Complete NT WT 33 CCTTTTCCTCAACCTGAACTTCCTTATCCTCAA gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) 3'Flanking NT WT 9 CCTCAACTT sequence Linker NT WT 51 GGCTCTGGATCTGGGTCCCTGGGATCTGGCTCTGGA TCTGGCTCTGGATCT HLA- NT WT 594 AGAGACTCTCCCGAGGATTTCGTGTACCAGTTTAAG DQB1*02:01 GGCATGTGCTACTTCACCAACGGGACAGAGCGCGT GCGTCTTGTGAGCAGAAGCATCTATAACCGAGAAG AGATCGTGCGCTTCGACAGCGACGTGGGGGAGTTC CGGGCGGTGACGCTGCTGGGGCTGCCTGCCGCCGA GTACTGGAACAGCCAGAAGGACATCCTGGAGAGGA AACGGGCGGCGGTGGACAGGGTGTGCAGACACAA CTACCAGTTGGAGCTCCGCACGACCTTGCAGCGGCG AGTGGAGCCCACAGTGACCATCTCCCCATCCAGGAC AGAGGCCCTCAACCACCACAACCTGCTGGTCTGCTC GGTGACAGATTTCTATCCAGCCCAGATCAAAGTCCG GTGGTTTCGGAATGACCAGGAGGAGACAGCTGGCG TTGTGTCCACCCCCCTTATTAGGAATGGTGACTGGA CCTTCCAGATCCTGGTGATGCTGGAAATGACTCCCC AGCGTGGAGACGTCTACACCTGCCACGTGGAGCAC CCCAGCCTCCAGAGCCCCATCACCGTGGAGTGGCG GGCTCAATCTGAATCTGCCCAGAGCAAG CD28 TM NT WT 78 TTTTGGGTGCTGGTGGTGGTTGGGGGAGTCCTGGC TTGCTATAGCTTGCTAGTAACAGTGGCCTTTATTATT TTCTGG CD28 co- NT WT 126 GTGAGGAGTAAGAGGAGCAGGCTCCTGCACAGTGA stimulatory CTACATGAACATGACTCCCCGCCGCCCCGGGCCCAC domain CCGCAAGCATTACCAGCCCTATGCCCCACCACGCGA CTTCGCAGCCTATCGCTCC CD3 zeta NT WT 336 AGAGTGAAGTTCAGCAGGAGCGCAGACGCCCCCGC primary GTACCAGCAGGGCCAGAACCAGCTCTATAACGAGC signaling TCAATCTAGGACGAAGAGAGGAGTACGATGTTTTG domain GACAAGAGACGTGGCCGGGACCCTGAGATGGGGG GAAAGCCGAGAAGGAAGAACCCTCAGGAAGGCCT GTACAATGAACTGCAGAAAGATAAGATGGCGGAGG CCTACAGTGAGATTGGGATGAAAGGCGAGCGCCGG AGGGGCAAGGGGCACGATGGCCTTTACCAGGGTCT CAGTACAGCCACCAAGGACACCTACGACGCCCTTCA CATGCAGGCCCTGCCCCCTCGC Linker NT WT 9 GGCAGCGGC viral self- NT WT 57 GCCACCAACTTCAGCCTGCTGAAGCAGGCCGGCGA cleaving 2A CGTGGAGGAAAACCCTGGGCCC polypeptide Signal NT WT 69 ATGATCCTAAACAAAGCTCTGATGCTGGGGGCCCTT peptide HLA- GCCCTGACCACCGTGATGAGCCCCTGTGGAGGT DQA1*05:01 HLA- NT WT 591 GAAGACATTGTGGCTGACCACGTCGCCTCTTATGGT DQA1*05:01 GTAAACTTGTACCAGTCTTACGGTCCCTCTGGCCAG TACACCCATGAATTTGATGGAGATGAGCAGTTCTAC GTGGACCTGGGGAGGAAGGAGACTGTCTGGTGTTT GCCTGTTCTCAGACAATTTAGATTTGACCCGCAATTT GCACTGACAAACATCGCTGTCCTAAAACATAACTTG AACAGTCTGATTAAACGCTCCAACTCTACCGCTGCT ACCAATGAGGTTCCTGAGGTCACAGTGTTTTCCAAG TCTCCCGTGACACTGGGTCAGCCCAACATCCTCATCT GTCTTGTGGACAACATCTTTCCTCCTGTGGTCAACAT CACATGGCTGAGCAATGGGCACTCAGTCACAGAAG GTGTTTCTGAGACCAGCTTCCTCTCCAAGAGTGATC ATTCCTTCTTCAAGATCAGTTACCTCACCCTCCTCCCT TCTGCTGAGGAGAGTTATGACTGCAAGGTGGAGCA CTGGGGCCTGGACAAGCCTCTTCTGAAACACTGGG AGCCTGAGATTCCAGCCCCTATGTCAGAGCTCACAG AGACTGTGGTCTGC CD28 TM NT WT 78 TTTTGGGTGCTGGTGGTGGTTGGGGGAGTCCTGGC TTGCTATAGCTTGCTAGTAACAGTGGCCTTTATTATT TTCTGG CD28 co- NT WT 126 GTGAGGAGTAAGAGGAGCAGGCTCCTGCACAGTGA stimulatory CTACATGAACATGACTCCCCGCCGCCCCGGGCCCAC domain CCGCAAGCATTACCAGCCCTATGCCCCACCACGCGA CTTCGCAGCCTATCGCTCC CD3 zeta NT WT 336 AGAGTGAAGTTCAGCAGGAGCGCAGACGCCCCCGC primary GTACCAGCAGGGCCAGAACCAGCTCTATAACGAGC signaling TCAATCTAGGACGAAGAGAGGAGTACGATGTTTTG domain GACAAGAGACGTGGCCGGGACCCTGAGATGGGGG GAAAGCCGAGAAGGAAGAACCCTCAGGAAGGCCT GTACAATGAACTGCAGAAAGATAAGATGGCGGAGG CCTACAGTGAGATTGGGATGAAAGGCGAGCGCCGG AGGGGCAAGGGGCACGATGGCCTTTACCAGGGTCT CAGTACAGCCACCAAGGACACCTACGACGCCCTTCA CATGCAGGCCCTGCCCCCTCGC stop NT WT 3 TGA CHAR_HLA- NT OPT 2601 ATGAGCTGGAAGAAAGCGCTGCGTATCCCGGGTGG DQ2.5-glia- CCTGCGTGCGGCGACCGTTACCCTGATGCTGAGCAT α1a-glia-α2 GCTGAGCACCCCGGTGGCGGAGGGTCAGCTGCAAC molecule (α- CGTTTCCGCAGCCGGAACTGCCGTACCCGCAGCCGC gliadin) AACTGGGTAGCGGTAGCGGTAGCCTGGGCAGCGGC AGCGGTAGCGGTAGCGGCAGCCGTGACAGCCCGG AGGATTTCGTTTACCAATTCAAGGGCATGTGCTACT TCACCAACGGCACCGAACGTGTGCGTCTGGTTAGCC GTAGCATCTACAACCGTGAGGAAATTGTGCGTTTCG ACAGCGATGTTGGCGAGTTTCGTGCGGTGACCCTG CTGGGTCTGCCGGCGGCGGAGTACTGGAACAGCCA GAAGGACATCCTGGAACGTAAACGTGCGGCGGTGG ATCGTGTTTGCCGTCACAACTATCAGCTGGAGCTGC GTACCACCCTGCAACGTCGTGTGGAACCGACCGTTA CCATCAGCCCGAGCCGTACCGAAGCGCTGAACCACC ACAACCTGCTGGTGTGCAGCGTTACCGACTTCTACC CGGCGCAGATTAAAGTTCGTTGGTTTCGTAACGATC AAGAGGAAACCGCGGGTGTGGTTAGCACCCCGCTG ATCCGTAACGGCGACTGGACCTTCCAGATTCTGGTT ATGCTGGAGATGACCCCGCAACGTGGTGATGTGTA CACCTGCCACGTTGAACACCCGAGCCTGCAGAGCCC GATTACCGTGGAGTGGCGTGCGCAGAGCGAAAGCG CGCAAAGCAAGTTTTGGGTTCTGGTGGTTGTGGGT GGCGTGCTGGCGTGCTACAGCCTGCTGGTGACCGT TGCGTTCATCATCTTCTGGGTGCGTAGCAAACGTAG CCGTCTGCTGCACAGCGACTATATGAACATGACCCC GCGTCGTCCGGGTCCGACCCGTAAGCACTACCAACC GTATGCGCCGCCGCGTGACTTTGCGGCGTACCGTA GCCGTGTTAAATTTAGCCGTAGCGCGGATGCGCCG GCGTACCAGCAGGGTCAGAACCAACTGTATAACGA GCTGAACCTGGGCCGTCGTGAGGAATATGACGTGC TGGATAAGCGTCGTGGTCGTGATCCGGAAATGGGT GGCAAGCCGCGTCGTAAAAACCCGCAGGAAGGTCT GTACAACGAACTGCAAAAGGACAAAATGGCGGAG GCGTATAGCGAAATTGGTATGAAGGGCGAGCGTCG TCGTGGTAAAGGCCACGATGGTCTGTACCAGGGCC TGAGCACCGCGACCAAAGACACCTATGATGCGCTG CACATGCAAGCGCTGCCGCCGCGTGGTAGCGGTGC GACCAACTTCAGCCTGCTGAAGCAGGCGGGTGACG TTGAGGAAAACCCGGGCCCGATGATCCTGAACAAA GCGCTGATGCTGGGTGCGCTGGCGCTGACCACCGT TATGAGCCCGTGCGGTGGCGAGGACATTGTGGCGG ATCACGTTGCGAGCTACGGCGTGAACCTGTACCAGA GCTATGGTCCGAGCGGCCAATACACCCACGAGTTCG ACGGTGATGAACAATTTTATGTTGACCTGGGCCGTA AGGAAACCGTGTGGTGCCTGCCGGTTCTGCGTCAG TTCCGTTTTGATCCGCAATTCGCGCTGACCAACATCG CGGTGCTGAAGCACAACCTGAACAGCCTGATTAAAC GTAGCAACAGCACCGCGGCGACCAACGAGGTTCCG GAAGTGACCGTTTTCAGCAAAAGCCCGGTGACCCTG GGTCAGCCGAACATCCTGATTTGCCTGGTTGACAAC ATCTTTCCGCCGGTTGTGAACATTACCTGGCTGAGC AACGGTCACAGCGTGACCGAGGGCGTTAGCGAAAC CAGCTTCCTGAGCAAGAGCGATCACAGCTTCTTTAA AATCAGCTATCTGACCCTGCTGCCGAGCGCGGAGG AAAGCTATGACTGCAAGGTGGAGCACTGGGGTCTG GATAAGCCGCTGCTGAAACACTGGGAGCCGGAAAT TCCGGCGCCGATGAGCGAGCTGACCGAAACCGTTG TGTGCTTTTGGGTTCTGGTTGTGGTTGGTGGCGTGT TAGCTTGCTATAGCCTGCTGGTTACCGTGGCGTTTA TTATCTTCTGGGTTCGCAGCAAGCGTAGCCGTCTGC TGCATAGCGATTACATGAATATGACCCCGCGTCGTC CTGGCCCGACCCGCAAACATTATCAACCGTACGCGC CGCCGCGTGACTTTGCAGCGTATCGTAGCCGTGTTA AGTTTAGCCGTAGCGCGGACGCGCCGGCGTATCAA CAGGGCCAAAATCAGCTGTACAATGAACTGAATCTG GGTCGTCGTGAAGAGTACGATGTTCTGGACAAACG TCGTGGTCGTGACCCGGAGATGGGTGGCAAACCGC GTCGTAAGAACCCGCAGGAAGGTTTATATAATGAG CTGCAGAAAGATAAGATGGCGGAAGCGTATAGCGA AATCGGTATGAAGGGCGAACGTCGTCGTGGCAAGG GTCATGACGGCCTGTATCAAGGTCTGAGCACCGCG ACCAAGGATACCTACGACGCGCTGCATATGCAGGC GCTGCCGCCGCGTTAA Signal NT OPT 96 ATGAGCTGGAAGAAAGCGCTGCGTATCCCGGGTGG peptide HLA- CCTGCGTGCGGCGACCGTTACCCTGATGCTGAGCAT DQB1*02:01 GCTGAGCACCCCGGTGGCGGAGGGT 5' Flanking NT OPT 9 CAGCTGCAA sequence HLA-DQ2- NT OPT 27 CCGTTTCCGCAGCCGGAACTGCCGTAC glia-α1a HLA-DQ2- NT OPT 27 CCGCAGCCGGAACTGCCGTACCCGCAG glia-α2 Complete NT OPT 33 CCGTTTCCGCAGCCGGAACTGCCGTACCCGCAG gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) 3'Flanking NT OPT 9 CCGCAACTG sequence Linker NT OPT 51 GGTAGCGGTAGCGGTAGCCTGGGCAGCGGCAGCG GTAGCGGTAGCGGCAGC HLA- NT OPT 594 CGTGACAGCCCGGAGGATTTCGTTTACCAATTCAAG DQB1*02:01 GGCATGTGCTACTTCACCAACGGCACCGAACGTGTG CGTCTGGTTAGCCGTAGCATCTACAACCGTGAGGAA ATTGTGCGTTTCGACAGCGATGTTGGCGAGTTTCGT GCGGTGACCCTGCTGGGTCTGCCGGCGGCGGAGTA CTGGAACAGCCAGAAGGACATCCTGGAACGTAAAC GTGCGGCGGTGGATCGTGTTTGCCGTCACAACTATC AGCTGGAGCTGCGTACCACCCTGCAACGTCGTGTG GAACCGACCGTTACCATCAGCCCGAGCCGTACCGAA GCGCTGAACCACCACAACCTGCTGGTGTGCAGCGTT ACCGACTTCTACCCGGCGCAGATTAAAGTTCGTTGG TTTCGTAACGATCAAGAGGAAACCGCGGGTGTGGT TAGCACCCCGCTGATCCGTAACGGCGACTGGACCTT CCAGATTCTGGTTATGCTGGAGATGACCCCGCAACG TGGTGATGTGTACACCTGCCACGTTGAACACCCGAG CCTGCAGAGCCCGATTACCGTGGAGTGGCGTGCGC AGAGCGAAAGCGCGCAAAGCAAG CD28 TM NT OPT 78 TTTTGGGTTCTGGTGGTTGTGGGTGGCGTGCTGGC GTGCTACAGCCTGCTGGTGACCGTTGCGTTCATCAT CTTCTGG CD28 co- NT OPT 126 GTGCGTAGCAAACGTAGCCGTCTGCTGCACAGCGA stimulatory CTATATGAACATGACCCCGCGTCGTCCGGGTCCGAC domain CCGTAAGCACTACCAACCGTATGCGCCGCCGCGTGA CTTTGCGGCGTACCGTAGC CD3 zeta NT OPT 336 CGTGTTAAATTTAGCCGTAGCGCGGATGCGCCGGC primary GTACCAGCAGGGTCAGAACCAACTGTATAACGAGC signaling TGAACCTGGGCCGTCGTGAGGAATATGACGTGCTG domain GATAAGCGTCGTGGTCGTGATCCGGAAATGGGTGG CAAGCCGCGTCGTAAAAACCCGCAGGAAGGTCTGT ACAACGAACTGCAAAAGGACAAAATGGCGGAGGC GTATAGCGAAATTGGTATGAAGGGCGAGCGTCGTC GTGGTAAAGGCCACGATGGTCTGTACCAGGGCCTG AGCACCGCGACCAAAGACACCTATGATGCGCTGCA CATGCAAGCGCTGCCGCCGCGT Linker NT OPT 9 GGTAGCGGT viral self- NT OPT 57 GCGACCAACTTCAGCCTGCTGAAGCAGGCGGGTGA cleaving 2A CGTTGAGGAAAACCCGGGCCCG polypeptide Signal NT OPT 69 ATGATCCTGAACAAAGCGCTGATGCTGGGTGCGCT peptide HLA- GGCGCTGACCACCGTTATGAGCCCGTGCGGTGGC DQA1*05:01 HLA- NT OPT 591 GAGGACATTGTGGCGGATCACGTTGCGAGCTACGG DQA1*05:01 CGTGAACCTGTACCAGAGCTATGGTCCGAGCGGCC AATACACCCACGAGTTCGACGGTGATGAACAATTTT ATGTTGACCTGGGCCGTAAGGAAACCGTGTGGTGC CTGCCGGTTCTGCGTCAGTTCCGTTTTGATCCGCAAT TCGCGCTGACCAACATCGCGGTGCTGAAGCACAACC TGAACAGCCTGATTAAACGTAGCAACAGCACCGCG GCGACCAACGAGGTTCCGGAAGTGACCGTTTTCAG CAAAAGCCCGGTGACCCTGGGTCAGCCGAACATCCT GATTTGCCTGGTTGACAACATCTTTCCGCCGGTTGT GAACATTACCTGGCTGAGCAACGGTCACAGCGTGA CCGAGGGCGTTAGCGAAACCAGCTTCCTGAGCAAG AGCGATCACAGCTTCTTTAAAATCAGCTATCTGACCC TGCTGCCGAGCGCGGAGGAAAGCTATGACTGCAAG GTGGAGCACTGGGGTCTGGATAAGCCGCTGCTGAA ACACTGGGAGCCGGAAATTCCGGCGCCGATGAGCG AGCTGACCGAAACCGTTGTGTGC 9 CD28 TM NT OPT 78 TTTTGGGTTCTGGTTGTGGTTGGTGGCGTGTTAGCT TGCTATAGCCTGCTGGTTACCGTGGCGTTTATTATCT TCTGG 0 CD28 co- NT OPT 126 GTTCGCAGCAAGCGTAGCCGTCTGCTGCATAGCGAT stimulatory TACATGAATATGACCCCGCGTCGTCCTGGCCCGACC domain CGCAAACATTATCAACCGTACGCGCCGCCGCGTGAC TTTGCAGCGTATCGTAGC 1 CD3 zeta NT OPT 336 CGTGTTAAGTTTAGCCGTAGCGCGGACGCGCCGGC primary GTATCAACAGGGCCAAAATCAGCTGTACAATGAACT signaling GAATCTGGGTCGTCGTGAAGAGTACGATGTTCTGG domain ACAAACGTCGTGGTCGTGACCCGGAGATGGGTGGC AAACCGCGTCGTAAGAACCCGCAGGAAGGTTTATA TAATGAGCTGCAGAAAGATAAGATGGCGGAAGCGT ATAGCGAAATCGGTATGAAGGGCGAACGTCGTCGT GGCAAGGGTCATGACGGCCTGTATCAAGGTCTGAG CACCGCGACCAAGGATACCTACGACGCGCTGCATAT GCAGGCGCTGCCGCCGCGT stop NT OPT 3 TAA Table 2: CHAR HLA-DQ2.5-glia-Ω1-glia-Ω2 molecule SEQ ID CHAR Amino Acid (AA), Length Sequence NO POLYPEPTIDE Nucleotide (NT) or Nucleotide Codon Optimised (NT OPT) 43 CHAR_HLA- AA 866 MSWKKALRIPGGLRAATVTLMLSMLSTPVAEGPQQP DQ2.5-glia- FPQPEQPFPWQPQGSGSGSLGSGSGSGSGSRDSPED Ω1-glia-Ω2 FVYQFKGMCYFTNGTERVRLVSRSIYNREEIVRFDSDV molecule (Ω- GEFRAVTLLGLPAAEYWNSQKDILERKRAAVDRVCRH gliadin) NYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSVT DFYPAQIKVRWFRNDQEETAGVVSTPLIRNGDWTFQI LVMLEMTPQRGDVYTCHVEHPSLQSPITVEWRAQSE SAQSKFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSR LLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRSR VKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDK RRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYS EIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQ ALPPRGSGATNFSLLKQAGDVEENPGPMILNKALML GALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPS GQYTHEFDGDEQFYVDLGRKETVWCLPVLRQFRFDP QFALTNIAVLKHNLNSLIKRSNSTAATNEVPEVTVFSKS PVTLGQPNILICLVDNIFPPVVNITWLSNGHSVTEGVS ETSFLSKSDHSFFKISYLTLLPSAEESYDCKVEHWGLDK PLLKHWEPEIPAPMSELTETVVCFWVLVVVGGVLACY SLLVTVAFIIFWVRSKRSRLLHSDYMNMTPRRPGPTRK HYQPYAPPRDFAAYRSRVKFSRSADAPAYQQGQNQL YNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQE GLYNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQG LSTATKDTYDALHMQALPPR Signal AA 32 MSWKKALRIPGGLRAATVTLMLSMLSTPVAEG peptide HLA- DQB1*02:01 5' Flanking AA 3 PQQ sequence HLA-DQ2- AA 9 PFPQPEQPF glia-Ω1 HLA-DQ2- AA 9 PQPEQPFPW glia-Ω2 Complete AA 11 PFPQPEQPFPW gliadin omega peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2- glia-Ω2) 3'Flanking AA 3 QPQ sequence Linker AA 17 GSGSGSLGSGSGSGSGS HLA- AA 198 RDSPEDFVYQFKGMCYFTNGTERVRLVSRSIYNREEIV DQB1*02:01 RFDSDVGEFRAVTLLGLPAAEYWNSQKDILERKRAAV DRVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNHHN LLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTPLIRN GDWTFQILVMLEMTPQRGDVYTCHVEHPSLQSPITV EWRAQSESAQSK CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW CD28 co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD primary KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY signaling SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQ domainALPPRLinker AA 3 GSG viral self- AA 19 ATNFSLLKQAGDVEENPGP cleaving 2A polypeptide Signal AA 23 MILNKALMLGALALTTVMSPCGG peptide HLA- DQA1*05:01 HLA- AA 197 EDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYV DQA1*05:01 DLGRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNS LIKRSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNI FPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYL TLLPSAEESYDCKVEHWGLDKPLLKHWEPEIPAPMSEL TETVVC CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW CD28 co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD primary KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY signaling SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQ domainALPPRStop AA 1 * CHAR_HLA- NT WT 2601 ATGAGCTGGAAGAAAGCGCTGCGTATCCCGGGTGG DQ2.5-glia- CCTGCGTGCGGCGACCGTTACCCTGATGCTGAGCAT Ω1-glia-Ω2 GCTGAGCACCCCGGTGGCGGAGGGTCCACAACAAC molecule (Ω- CTTTTCCACAGCCGGAACAACCATTTCCCTGGCAAC gliadin) CACAAGGTAGCGGTAGCGGTAGCCTGGGCAGCGG CAGCGGTAGCGGTAGCGGCAGCCGTGACAGCCCG GAGGATTTCGTTTACCAATTCAAGGGCATGTGCTAC TTCACCAACGGCACCGAACGTGTGCGTCTGGTTAGC CGTAGCATCTACAACCGTGAGGAAATTGTGCGTTTC GACAGCGATGTTGGCGAGTTTCGTGCGGTGACCCT GCTGGGTCTGCCGGCGGCGGAGTACTGGAACAGCC AGAAGGACATCCTGGAACGTAAACGTGCGGCGGTG GATCGTGTTTGCCGTCACAACTATCAGCTGGAGCTG CGTACCACCCTGCAACGTCGTGTGGAACCGACCGTT ACCATCAGCCCGAGCCGTACCGAAGCGCTGAACCA CCACAACCTGCTGGTGTGCAGCGTTACCGACTTCTA CCCGGCGCAGATTAAAGTTCGTTGGTTTCGTAACGA TCAAGAGGAAACCGCGGGTGTGGTTAGCACCCCGC TGATCCGTAACGGCGACTGGACCTTCCAGATTCTGG TTATGCTGGAGATGACCCCGCAACGTGGTGATGTGT ACACCTGCCACGTTGAACACCCGAGCCTGCAGAGCC CGATTACCGTGGAGTGGCGTGCGCAGAGCGAAAGC GCGCAAAGCAAGTTTTGGGTTCTGGTGGTTGTGGG TGGCGTGCTGGCGTGCTACAGCCTGCTGGTGACCG TTGCGTTCATCATCTTCTGGGTGCGTAGCAAACGTA GCCGTCTGCTGCACAGCGACTATATGAACATGACCC CGCGTCGTCCGGGTCCGACCCGTAAGCACTACCAAC CGTATGCGCCGCCGCGTGACTTTGCGGCGTACCGTA GCCGTGTTAAATTTAGCCGTAGCGCGGATGCGCCG GCGTACCAGCAGGGTCAGAACCAACTGTATAACGA GCTGAACCTGGGCCGTCGTGAGGAATATGACGTGC TGGATAAGCGTCGTGGTCGTGATCCGGAAATGGGT GGCAAGCCGCGTCGTAAAAACCCGCAGGAAGGTCT GTACAACGAACTGCAAAAGGACAAAATGGCGGAG GCGTATAGCGAAATTGGTATGAAGGGCGAGCGTCG TCGTGGTAAAGGCCACGATGGTCTGTACCAGGGCC TGAGCACCGCGACCAAAGACACCTATGATGCGCTG CACATGCAAGCGCTGCCGCCGCGTGGTAGCGGTGC GACCAACTTCAGCCTGCTGAAGCAGGCGGGTGACG TTGAGGAAAACCCGGGCCCGATGATCCTGAACAAA GCGCTGATGCTGGGTGCGCTGGCGCTGACCACCGT TATGAGCCCGTGCGGTGGCGAGGACATTGTGGCGG ATCACGTTGCGAGCTACGGCGTGAACCTGTACCAG AGCTATGGTCCGAGCGGCCAATACACCCACGAGTTC GACGGTGATGAACAATTTTATGTTGACCTGGGCCGT AAGGAAACCGTGTGGTGCCTGCCGGTTCTGCGTCA GTTCCGTTTTGATCCGCAATTCGCGCTGACCAACATC GCGGTGCTGAAGCACAACCTGAACAGCCTGATTAA ACGTAGCAACAGCACCGCGGCGACCAACGAGGTTC CGGAAGTGACCGTTTTCAGCAAAAGCCCGGTGACC CTGGGTCAGCCGAACATCCTGATTTGCCTGGTTGAC AACATCTTTCCGCCGGTTGTGAACATTACCTGGCTG AGCAACGGTCACAGCGTGACCGAGGGCGTTAGCGA AACCAGCTTCCTGAGCAAGAGCGATCACAGCTTCTT TAAAATCAGCTATCTGACCCTGCTGCCGAGCGCGGA GGAAAGCTATGACTGCAAGGTGGAGCACTGGGGTC TGGATAAGCCGCTGCTGAAACACTGGGAGCCGGAA ATTCCGGCGCCGATGAGCGAGCTGACCGAAACCGT TGTGTGCTTTTGGGTTCTGGTTGTGGTTGGTGGCGT GTTAGCTTGCTATAGCCTGCTGGTTACCGTGGCGTT TATTATCTTCTGGGTTCGCAGCAAGCGTAGCCGTCT GCTGCATAGCGATTACATGAATATGACCCCGCGTCG TCCTGGCCCGACCCGCAAACATTATCAACCGTACGC GCCGCCGCGTGACTTTGCAGCGTATCGTAGCCGTGT TAAGTTTAGCCGTAGCGCGGACGCGCCGGCGTATC AACAGGGCCAAAATCAGCTGTACAATGAACTGAAT CTGGGTCGTCGTGAAGAGTACGATGTTCTGGACAA ACGTCGTGGTCGTGACCCGGAGATGGGTGGCAAAC CGCGTCGTAAGAACCCGCAGGAAGGTTTATATAAT GAGCTGCAGAAAGATAAGATGGCGGAAGCGTATA GCGAAATCGGTATGAAGGGCGAACGTCGTCGTGGC AAGGGTCATGACGGCCTGTATCAAGGTCTGAGCAC CGCGACCAAGGATACCTACGACGCGCTGCATATGC AGGCGCTGCCGCCGCGTTAA Signal NT WT 96 ATGTCTTGGAAAAAGGCTTTGCGGATCCCCGGAGG peptide HLA- CCTTCGGGCAGCAACTGTGACCTTGATGCTGTCGAT DQB1*02:01 GCTGAGCACCCCAGTGGCTGAGGGC 5' Flanking NT WT 9 CCACAACAA sequence HLA-DQ2- NT WT 27 CCTTTTCCACAGCCGGAACAACCATTT glia-Ω1 HLA-DQ2- NT WT 27 CCACAGCCGGAACAACCATTTCCCTGG glia-Ω2 Complete NT WT 33 CCTTTTCCACAGCCGGAACAACCATTTCCCTGG gliadin peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2- glia-Ω2) 3'Flanking NT WT 9 CAACCACAA sequence Linker NT WT 51 GGCTCTGGATCTGGGTCCCTGGGATCTGGCTCTGG ATCTGGCTCTGGATCT HLA- NT WT 594 AGAGACTCTCCCGAGGATTTCGTGTACCAGTTTAAG DQB1*02:01 GGCATGTGCTACTTCACCAACGGGACAGAGCGCGT GCGTCTTGTGAGCAGAAGCATCTATAACCGAGAAG AGATCGTGCGCTTCGACAGCGACGTGGGGGAGTTC CGGGCGGTGACGCTGCTGGGGCTGCCTGCCGCCGA GTACTGGAACAGCCAGAAGGACATCCTGGAGAGGA AACGGGCGGCGGTGGACAGGGTGTGCAGACACAA CTACCAGTTGGAGCTCCGCACGACCTTGCAGCGGC GAGTGGAGCCCACAGTGACCATCTCCCCATCCAGG ACAGAGGCCCTCAACCACCACAACCTGCTGGTCTGC TCGGTGACAGATTTCTATCCAGCCCAGATCAAAGTC CGGTGGTTTCGGAATGACCAGGAGGAGACAGCTGG CGTTGTGTCCACCCCCCTTATTAGGAATGGTGACTG GACCTTCCAGATCCTGGTGATGCTGGAAATGACTCC CCAGCGTGGAGACGTCTACACCTGCCACGTGGAGC ACCCCAGCCTCCAGAGCCCCATCACCGTGGAGTGGC GGGCTCAATCTGAATCTGCCCAGAGCAAG CD28 TM NT WT 78 TTTTGGGTGCTGGTGGTGGTTGGGGGAGTCCTGGC TTGCTATAGCTTGCTAGTAACAGTGGCCTTTATTATT TTCTGG CD28 co- NT WT 126 GTGAGGAGTAAGAGGAGCAGGCTCCTGCACAGTG stimulatory ACTACATGAACATGACTCCCCGCCGCCCCGGGCCCA domain CCCGCAAGCATTACCAGCCCTATGCCCCACCACGCG ACTTCGCAGCCTATCGCTCC CD3 zeta NT WT 336 AGAGTGAAGTTCAGCAGGAGCGCAGACGCCCCCGC primary GTACCAGCAGGGCCAGAACCAGCTCTATAACGAGC signaling TCAATCTAGGACGAAGAGAGGAGTACGATGTTTTG domain GACAAGAGACGTGGCCGGGACCCTGAGATGGGGG GAAAGCCGAGAAGGAAGAACCCTCAGGAAGGCCT GTACAATGAACTGCAGAAAGATAAGATGGCGGAG GCCTACAGTGAGATTGGGATGAAAGGCGAGCGCCG GAGGGGCAAGGGGCACGATGGCCTTTACCAGGGTC TCAGTACAGCCACCAAGGACACCTACGACGCCCTTC ACATGCAGGCCCTGCCCCCTCGC Linker NT WT 9 GGCAGCGGC viral self- NT WT 57 GCCACCAACTTCAGCCTGCTGAAGCAGGCCGGCGA cleaving 2A CGTGGAGGAAAACCCTGGGCCC polypeptide Signal NT WT 69 ATGATCCTAAACAAAGCTCTGATGCTGGGGGCCCTT peptide HLA- GCCCTGACCACCGTGATGAGCCCCTGTGGAGGT DQA1*05:01 HLA- NT WT 591 GAAGACATTGTGGCTGACCACGTCGCCTCTTATGGT DQA1*05:01 GTAAACTTGTACCAGTCTTACGGTCCCTCTGGCCAG TACACCCATGAATTTGATGGAGATGAGCAGTTCTAC GTGGACCTGGGGAGGAAGGAGACTGTCTGGTGTTT GCCTGTTCTCAGACAATTTAGATTTGACCCGCAATTT GCACTGACAAACATCGCTGTCCTAAAACATAACTTG AACAGTCTGATTAAACGCTCCAACTCTACCGCTGCT ACCAATGAGGTTCCTGAGGTCACAGTGTTTTCCAAG TCTCCCGTGACACTGGGTCAGCCCAACATCCTCATCT GTCTTGTGGACAACATCTTTCCTCCTGTGGTCAACAT CACATGGCTGAGCAATGGGCACTCAGTCACAGAAG GTGTTTCTGAGACCAGCTTCCTCTCCAAGAGTGATC ATTCCTTCTTCAAGATCAGTTACCTCACCCTCCTCCCT TCTGCTGAGGAGAGTTATGACTGCAAGGTGGAGCA CTGGGGCCTGGACAAGCCTCTTCTGAAACACTGGG AGCCTGAGATTCCAGCCCCTATGTCAGAGCTCACAG AGACTGTGGTCTGC CD28 TM NT WT 78 TTTTGGGTGCTGGTGGTGGTTGGGGGAGTCCTGGC TTGCTATAGCTTGCTAGTAACAGTGGCCTTTATTATT TTCTGG CD28 co- NT WT 126 GTGAGGAGTAAGAGGAGCAGGCTCCTGCACAGTG stimulatory ACTACATGAACATGACTCCCCGCCGCCCCGGGCCCA domain CCCGCAAGCATTACCAGCCCTATGCCCCACCACGCG ACTTCGCAGCCTATCGCTCC CD3 zeta NT WT 336 AGAGTGAAGTTCAGCAGGAGCGCAGACGCCCCCGC primary GTACCAGCAGGGCCAGAACCAGCTCTATAACGAGC signaling TCAATCTAGGACGAAGAGAGGAGTACGATGTTTTG domain GACAAGAGACGTGGCCGGGACCCTGAGATGGGGG GAAAGCCGAGAAGGAAGAACCCTCAGGAAGGCCT GTACAATGAACTGCAGAAAGATAAGATGGCGGAG GCCTACAGTGAGATTGGGATGAAAGGCGAGCGCCG GAGGGGCAAGGGGCACGATGGCCTTTACCAGGGTC TCAGTACAGCCACCAAGGACACCTACGACGCCCTTC ACATGCAGGCCCTGCCCCCTCGC Stop NT WT 3 TGA CHAR_HLA- NT OPT 2601 ATGAGCTGGAAGAAAGCGCTGCGTATCCCGGGTGG DQ2.5-glia- CCTGCGTGCGGCGACCGTTACCCTGATGCTGAGCAT Ω1-glia-Ω2 GCTGAGCACCCCGGTGGCGGAGGGTCCACAGCAGC molecule (Ω- CCTTCCCTCAGCCAGAGCAGCCCTTTCCTTGGCAGC gliadin) CCCAGGGTAGCGGTAGCGGTAGCCTGGGCAGCGG CAGCGGTAGCGGTAGCGGCAGCCGTGACAGCCCG GAGGATTTCGTTTACCAATTCAAGGGCATGTGCTAC TTCACCAACGGCACCGAACGTGTGCGTCTGGTTAGC CGTAGCATCTACAACCGTGAGGAAATTGTGCGTTTC GACAGCGATGTTGGCGAGTTTCGTGCGGTGACCCT GCTGGGTCTGCCGGCGGCGGAGTACTGGAACAGCC AGAAGGACATCCTGGAACGTAAACGTGCGGCGGTG GATCGTGTTTGCCGTCACAACTATCAGCTGGAGCTG ĵĶ CGTACCACCCTGCAACGTCGTGTGGAACCGACCGTT ACCATCAGCCCGAGCCGTACCGAAGCGCTGAACCA CCACAACCTGCTGGTGTGCAGCGTTACCGACTTCTA CCCGGCGCAGATTAAAGTTCGTTGGTTTCGTAACGA TCAAGAGGAAACCGCGGGTGTGGTTAGCACCCCGC TGATCCGTAACGGCGACTGGACCTTCCAGATTCTGG TTATGCTGGAGATGACCCCGCAACGTGGTGATGTGT ACACCTGCCACGTTGAACACCCGAGCCTGCAGAGCC CGATTACCGTGGAGTGGCGTGCGCAGAGCGAAAGC GCGCAAAGCAAGTTTTGGGTTCTGGTGGTTGTGGG TGGCGTGCTGGCGTGCTACAGCCTGCTGGTGACCG TTGCGTTCATCATCTTCTGGGTGCGTAGCAAACGTA GCCGTCTGCTGCACAGCGACTATATGAACATGACCC CGCGTCGTCCGGGTCCGACCCGTAAGCACTACCAAC CGTATGCGCCGCCGCGTGACTTTGCGGCGTACCGTA GCCGTGTTAAATTTAGCCGTAGCGCGGATGCGCCG GCGTACCAGCAGGGTCAGAACCAACTGTATAACGA GCTGAACCTGGGCCGTCGTGAGGAATATGACGTGC TGGATAAGCGTCGTGGTCGTGATCCGGAAATGGGT GGCAAGCCGCGTCGTAAAAACCCGCAGGAAGGTCT GTACAACGAACTGCAAAAGGACAAAATGGCGGAG GCGTATAGCGAAATTGGTATGAAGGGCGAGCGTCG TCGTGGTAAAGGCCACGATGGTCTGTACCAGGGCC TGAGCACCGCGACCAAAGACACCTATGATGCGCTG CACATGCAAGCGCTGCCGCCGCGTGGTAGCGGTGC GACCAACTTCAGCCTGCTGAAGCAGGCGGGTGACG TTGAGGAAAACCCGGGCCCGATGATCCTGAACAAA GCGCTGATGCTGGGTGCGCTGGCGCTGACCACCGT TATGAGCCCGTGCGGTGGCGAGGACATTGTGGCGG ATCACGTTGCGAGCTACGGCGTGAACCTGTACCAG AGCTATGGTCCGAGCGGCCAATACACCCACGAGTTC GACGGTGATGAACAATTTTATGTTGACCTGGGCCGT AAGGAAACCGTGTGGTGCCTGCCGGTTCTGCGTCA GTTCCGTTTTGATCCGCAATTCGCGCTGACCAACATC GCGGTGCTGAAGCACAACCTGAACAGCCTGATTAA ACGTAGCAACAGCACCGCGGCGACCAACGAGGTTC CGGAAGTGACCGTTTTCAGCAAAAGCCCGGTGACC CTGGGTCAGCCGAACATCCTGATTTGCCTGGTTGAC AACATCTTTCCGCCGGTTGTGAACATTACCTGGCTG AGCAACGGTCACAGCGTGACCGAGGGCGTTAGCGA AACCAGCTTCCTGAGCAAGAGCGATCACAGCTTCTT TAAAATCAGCTATCTGACCCTGCTGCCGAGCGCGGA GGAAAGCTATGACTGCAAGGTGGAGCACTGGGGTC TGGATAAGCCGCTGCTGAAACACTGGGAGCCGGAA ATTCCGGCGCCGATGAGCGAGCTGACCGAAACCGT TGTGTGCTTTTGGGTTCTGGTTGTGGTTGGTGGCGT GTTAGCTTGCTATAGCCTGCTGGTTACCGTGGCGTT TATTATCTTCTGGGTTCGCAGCAAGCGTAGCCGTCT GCTGCATAGCGATTACATGAATATGACCCCGCGTCG TCCTGGCCCGACCCGCAAACATTATCAACCGTACGC GCCGCCGCGTGACTTTGCAGCGTATCGTAGCCGTGT TAAGTTTAGCCGTAGCGCGGACGCGCCGGCGTATC AACAGGGCCAAAATCAGCTGTACAATGAACTGAAT CTGGGTCGTCGTGAAGAGTACGATGTTCTGGACAA ACGTCGTGGTCGTGACCCGGAGATGGGTGGCAAAC CGCGTCGTAAGAACCCGCAGGAAGGTTTATATAAT GAGCTGCAGAAAGATAAGATGGCGGAAGCGTATA GCGAAATCGGTATGAAGGGCGAACGTCGTCGTGGC AAGGGTCATGACGGCCTGTATCAAGGTCTGAGCAC CGCGACCAAGGATACCTACGACGCGCTGCATATGC AGGCGCTGCCGCCGCGTTAA Signal NT OPT 96 ATGAGCTGGAAGAAAGCGCTGCGTATCCCGGGTGG peptide HLA- CCTGCGTGCGGCGACCGTTACCCTGATGCTGAGCAT DQB1*02:01 GCTGAGCACCCCGGTGGCGGAGGGT 5' Flanking NT OPT 9 CCACAGCAG sequence HLA-DQ2- NT OPT 27 CCCTTCCCTCAGCCAGAGCAGCCCTTT glia-Ω1 HLA-DQ2- NT OPT 27 CCTCAGCCAGAGCAGCCCTTTCCTTGG glia-Ω2 Complete NT OPT 33 CCCTTCCCTCAGCCAGAGCAGCCCTTTCCTTGG gliadin peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2- glia-Ω2) 3'Flanking NT OPT 9 CAGCCCCAG sequence Linker NT OPT 51 GGTAGCGGTAGCGGTAGCCTGGGCAGCGGCAGCG GTAGCGGTAGCGGCAGC HLA- NT OPT 594 CGTGACAGCCCGGAGGATTTCGTTTACCAATTCAAG DQB1*02:01 GGCATGTGCTACTTCACCAACGGCACCGAACGTGTG CGTCTGGTTAGCCGTAGCATCTACAACCGTGAGGAA ATTGTGCGTTTCGACAGCGATGTTGGCGAGTTTCGT GCGGTGACCCTGCTGGGTCTGCCGGCGGCGGAGTA CTGGAACAGCCAGAAGGACATCCTGGAACGTAAAC GTGCGGCGGTGGATCGTGTTTGCCGTCACAACTATC AGCTGGAGCTGCGTACCACCCTGCAACGTCGTGTG GAACCGACCGTTACCATCAGCCCGAGCCGTACCGA AGCGCTGAACCACCACAACCTGCTGGTGTGCAGCG TTACCGACTTCTACCCGGCGCAGATTAAAGTTCGTT GGTTTCGTAACGATCAAGAGGAAACCGCGGGTGTG GTTAGCACCCCGCTGATCCGTAACGGCGACTGGACC TTCCAGATTCTGGTTATGCTGGAGATGACCCCGCAA CGTGGTGATGTGTACACCTGCCACGTTGAACACCCG AGCCTGCAGAGCCCGATTACCGTGGAGTGGCGTGC GCAGAGCGAAAGCGCGCAAAGCAAG CD28 TM NT OPT 78 TTTTGGGTTCTGGTGGTTGTGGGTGGCGTGCTGGC GTGCTACAGCCTGCTGGTGACCGTTGCGTTCATCAT CTTCTGG CD28 co- NT OPT 126 GTGCGTAGCAAACGTAGCCGTCTGCTGCACAGCGA stimulatory CTATATGAACATGACCCCGCGTCGTCCGGGTCCGAC domain CCGTAAGCACTACCAACCGTATGCGCCGCCGCGTGA CTTTGCGGCGTACCGTAGC CD3 zeta NT OPT 336 CGTGTTAAATTTAGCCGTAGCGCGGATGCGCCGGC primary GTACCAGCAGGGTCAGAACCAACTGTATAACGAGC signaling TGAACCTGGGCCGTCGTGAGGAATATGACGTGCTG domain GATAAGCGTCGTGGTCGTGATCCGGAAATGGGTGG CAAGCCGCGTCGTAAAAACCCGCAGGAAGGTCTGT ACAACGAACTGCAAAAGGACAAAATGGCGGAGGC GTATAGCGAAATTGGTATGAAGGGCGAGCGTCGTC GTGGTAAAGGCCACGATGGTCTGTACCAGGGCCTG AGCACCGCGACCAAAGACACCTATGATGCGCTGCA CATGCAAGCGCTGCCGCCGCGT Linker NT OPT 9 GGTAGCGGT viral self- NT OPT 57 GCGACCAACTTCAGCCTGCTGAAGCAGGCGGGTGA cleaving 2A CGTTGAGGAAAACCCGGGCCCG polypeptide Signal NT OPT 69 ATGATCCTGAACAAAGCGCTGATGCTGGGTGCGCT peptide HLA- GGCGCTGACCACCGTTATGAGCCCGTGCGGTGGC DQA1*05:01 HLA- NT OPT 591 GAGGACATTGTGGCGGATCACGTTGCGAGCTACGG DQA1*05:01 CGTGAACCTGTACCAGAGCTATGGTCCGAGCGGCC AATACACCCACGAGTTCGACGGTGATGAACAATTTT ATGTTGACCTGGGCCGTAAGGAAACCGTGTGGTGC CTGCCGGTTCTGCGTCAGTTCCGTTTTGATCCGCAAT TCGCGCTGACCAACATCGCGGTGCTGAAGCACAAC CTGAACAGCCTGATTAAACGTAGCAACAGCACCGC GGCGACCAACGAGGTTCCGGAAGTGACCGTTTTCA GCAAAAGCCCGGTGACCCTGGGTCAGCCGAACATC CTGATTTGCCTGGTTGACAACATCTTTCCGCCGGTT GTGAACATTACCTGGCTGAGCAACGGTCACAGCGT GACCGAGGGCGTTAGCGAAACCAGCTTCCTGAGCA AGAGCGATCACAGCTTCTTTAAAATCAGCTATCTGA CCCTGCTGCCGAGCGCGGAGGAAAGCTATGACTGC AAGGTGGAGCACTGGGGTCTGGATAAGCCGCTGCT GAAACACTGGGAGCCGGAAATTCCGGCGCCGATGA GCGAGCTGACCGAAACCGTTGTGTGC CD28 TM NT OPT 78 TTTTGGGTTCTGGTTGTGGTTGGTGGCGTGTTAGCT TGCTATAGCCTGCTGGTTACCGTGGCGTTTATTATCT TCTGG CD28 co- NT OPT 126 GTTCGCAGCAAGCGTAGCCGTCTGCTGCATAGCGAT stimulatory TACATGAATATGACCCCGCGTCGTCCTGGCCCGACC domain CGCAAACATTATCAACCGTACGCGCCGCCGCGTGAC TTTGCAGCGTATCGTAGC CD3 zeta NT OPT 336 CGTGTTAAGTTTAGCCGTAGCGCGGACGCGCCGGC primary GTATCAACAGGGCCAAAATCAGCTGTACAATGAACT signaling GAATCTGGGTCGTCGTGAAGAGTACGATGTTCTGG domain ACAAACGTCGTGGTCGTGACCCGGAGATGGGTGGC AAACCGCGTCGTAAGAACCCGCAGGAAGGTTTATA TAATGAGCTGCAGAAAGATAAGATGGCGGAAGCGT ATAGCGAAATCGGTATGAAGGGCGAACGTCGTCGT GGCAAGGGTCATGACGGCCTGTATCAAGGTCTGAG CACCGCGACCAAGGATACCTACGACGCGCTGCATAT GCAGGCGCTGCCGCCGCGT stop NT OPT 3 TAA Table 3: CHAR HLA-DQ2.5-gliadin-Ω-gliadin-α molecule SEQ ID CHAR Amino Acid (AA), Length Sequence NO POLYPEPTIDE Nucleotide (NT) or Nucleotide Codon Optimised (NT OPT) 5 CHAR_HLA- AA 888 MSWKKALRIPGGLRAATVTLMLSMLSTPVAEGPQQP DQ2.5-glia- FPQPEQPFPWQPQGGGGGQLQPFPQPELPYPQPQL Ω1Ω2-glia- GSGSGSLGSGSGSGSGSRDSPEDFVYQFKGMCYFTN α1α2 GTERVRLVSRSIYNREEIVRFDSDVGEFRAVTLLGLPAA molecule (Ω- EYWNSQKDILERKRAAVDRVCRHNYQLELRTTLQRRV gliadin and EPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFR α-gliadin) NDQEETAGVVSTPLIRNGDWTFQILVMLEMTPQRGD VYTCHVEHPSLQSPITVEWRAQSESAQSKFWVLVVVG GVLACYSLLVTVAFIIFWVRSKRSRLLHSDYMNMTPRR PGPTRKHYQPYAPPRDFAAYRSRVKFSRSADAPAYQQ GQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRR KNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHD GLYQGLSTATKDTYDALHMQALPPRGSGATNFSLLKQ AGDVEENPGPMILNKALMLGALALTTVMSPCGGEDI VADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDL GRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNSLIK RSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFP PVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLL PSAEESYDCKVEHWGLDKPLLKHWEPEIPAPMSELTE TVVCFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRL LHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRSRV KFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKR RGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEI GMKGERRRGKGHDGLYQGLSTATKDTYDALHMQAL PPR 2 Signal AA 32 MSWKKALRIPGGLRAATVTLMLSMLSTPVAEG peptide HLA- DQB1*02:01 5' Flanking AA 3 PQQ sequence 44 HLA-DQ2- AA 9 PFPQPEQPF glia-Ω1 45 HLA-DQ2- AA 9 PQPEQPFPW glia-Ω2 6 Complete AA 11 PFPQPEQPFPW gliadin omega peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2-glia-Ω2)3'Flanking AA 3 QPQ sequence Linker 5xG AA 5 GGGGG 5' Flanking AA 3 QLQ sequence HLA-DQ2- AA 9 PFPQPELPY glia-α1a HLA-DQ2- AA 9 PQPELPYPQ glia-α2 Complete AA 11 PFPQPELPYPQ alpha gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) 3'Flanking AA 3 PQL sequence Linker AA 17 GSGSGSLGSGSGSGSGS HLA- AA 198 RDSPEDFVYQFKGMCYFTNGTERVRLVSRSIYNREEIV DQB1*02:01 RFDSDVGEFRAVTLLGLPAAEYWNSQKDILERKRAAV EC DRVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNHHN LLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTPLIRN GDWTFQILVMLEMTPQRGDVYTCHVEHPSLQSPITV EWRAQSESAQSK CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW CD28 co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD primary KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY signaling SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQ domainALPPRLinker AA 3 GSG viral self- AA 19 ATNFSLLKQAGDVEENPGP cleaving 2A polypeptide Signal AA 23 MILNKALMLGALALTTVMSPCGG peptide HLA- DQA1*05:01 HLA- AA 197 EDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYV DQA1*05:01 DLGRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNS LIKRSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNI FPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYL TLLPSAEESYDCKVEHWGLDKPLLKHWEPEIPAPMSEL TETVVC CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW CD28 co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD primary KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY signaling SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQ domainALPPRStop AA 1 * CHAR_HLA- NT WT 2667 ATGAGCTGGAAGAAAGCGCTGCGTATCCCGGGTGG DQ2.5-glia- CCTGCGTGCGGCGACCGTTACCCTGATGCTGAGCAT Ω1Ω2-glia- GCTGAGCACCCCGGTGGCGGAGGGTCCACAACAAC α1α2 CTTTTCCACAGCCGGAACAACCATTTCCCTGGCAAC molecule (Ω- CACAAGGTGGTGGTGGTGGTCAACTTCAACCTTTTC gliadin and CTCAACCTGAACTTCCTTATCCTCAACCTCAACTTGG α-gliadin) TAGCGGTAGCGGTAGCCTGGGCAGCGGCAGCGGT AGCGGTAGCGGCAGCCGTGACAGCCCGGAGGATTT CGTTTACCAATTCAAGGGCATGTGCTACTTCACCAA CGGCACCGAACGTGTGCGTCTGGTTAGCCGTAGCA TCTACAACCGTGAGGAAATTGTGCGTTTCGACAGCG ATGTTGGCGAGTTTCGTGCGGTGACCCTGCTGGGTC TGCCGGCGGCGGAGTACTGGAACAGCCAGAAGGA CATCCTGGAACGTAAACGTGCGGCGGTGGATCGTG TTTGCCGTCACAACTATCAGCTGGAGCTGCGTACCA CCCTGCAACGTCGTGTGGAACCGACCGTTACCATCA GCCCGAGCCGTACCGAAGCGCTGAACCACCACAAC CTGCTGGTGTGCAGCGTTACCGACTTCTACCCGGCG CAGATTAAAGTTCGTTGGTTTCGTAACGATCAAGAG GAAACCGCGGGTGTGGTTAGCACCCCGCTGATCCG TAACGGCGACTGGACCTTCCAGATTCTGGTTATGCT GGAGATGACCCCGCAACGTGGTGATGTGTACACCT GCCACGTTGAACACCCGAGCCTGCAGAGCCCGATT ACCGTGGAGTGGCGTGCGCAGAGCGAAAGCGCGC AAAGCAAGTTTTGGGTTCTGGTGGTTGTGGGTGGC GTGCTGGCGTGCTACAGCCTGCTGGTGACCGTTGC GTTCATCATCTTCTGGGTGCGTAGCAAACGTAGCCG TCTGCTGCACAGCGACTATATGAACATGACCCCGCG TCGTCCGGGTCCGACCCGTAAGCACTACCAACCGTA TGCGCCGCCGCGTGACTTTGCGGCGTACCGTAGCC GTGTTAAATTTAGCCGTAGCGCGGATGCGCCGGCG TACCAGCAGGGTCAGAACCAACTGTATAACGAGCT GAACCTGGGCCGTCGTGAGGAATATGACGTGCTGG ATAAGCGTCGTGGTCGTGATCCGGAAATGGGTGGC AAGCCGCGTCGTAAAAACCCGCAGGAAGGTCTGTA CAACGAACTGCAAAAGGACAAAATGGCGGAGGCGT ATAGCGAAATTGGTATGAAGGGCGAGCGTCGTCGT GGTAAAGGCCACGATGGTCTGTACCAGGGCCTGAG CACCGCGACCAAAGACACCTATGATGCGCTGCACAT GCAAGCGCTGCCGCCGCGTGGTAGCGGTGCGACCA ACTTCAGCCTGCTGAAGCAGGCGGGTGACGTTGAG GAAAACCCGGGCCCGATGATCCTGAACAAAGCGCT GATGCTGGGTGCGCTGGCGCTGACCACCGTTATGA GCCCGTGCGGTGGCGAGGACATTGTGGCGGATCAC GTTGCGAGCTACGGCGTGAACCTGTACCAGAGCTA TGGTCCGAGCGGCCAATACACCCACGAGTTCGACG GTGATGAACAATTTTATGTTGACCTGGGCCGTAAGG AAACCGTGTGGTGCCTGCCGGTTCTGCGTCAGTTCC GTTTTGATCCGCAATTCGCGCTGACCAACATCGCGG TGCTGAAGCACAACCTGAACAGCCTGATTAAACGTA GCAACAGCACCGCGGCGACCAACGAGGTTCCGGAA GTGACCGTTTTCAGCAAAAGCCCGGTGACCCTGGGT CAGCCGAACATCCTGATTTGCCTGGTTGACAACATC TTTCCGCCGGTTGTGAACATTACCTGGCTGAGCAAC GGTCACAGCGTGACCGAGGGCGTTAGCGAAACCAG CTTCCTGAGCAAGAGCGATCACAGCTTCTTTAAAAT CAGCTATCTGACCCTGCTGCCGAGCGCGGAGGAAA GCTATGACTGCAAGGTGGAGCACTGGGGTCTGGAT AAGCCGCTGCTGAAACACTGGGAGCCGGAAATTCC GGCGCCGATGAGCGAGCTGACCGAAACCGTTGTGT GCTTTTGGGTTCTGGTTGTGGTTGGTGGCGTGTTAG CTTGCTATAGCCTGCTGGTTACCGTGGCGTTTATTAT CTTCTGGGTTCGCAGCAAGCGTAGCCGTCTGCTGCA TAGCGATTACATGAATATGACCCCGCGTCGTCCTGG CCCGACCCGCAAACATTATCAACCGTACGCGCCGCC GCGTGACTTTGCAGCGTATCGTAGCCGTGTTAAGTT TAGCCGTAGCGCGGACGCGCCGGCGTATCAACAGG GCCAAAATCAGCTGTACAATGAACTGAATCTGGGTC GTCGTGAAGAGTACGATGTTCTGGACAAACGTCGT GGTCGTGACCCGGAGATGGGTGGCAAACCGCGTCG TAAGAACCCGCAGGAAGGTTTATATAATGAGCTGC AGAAAGATAAGATGGCGGAAGCGTATAGCGAAATC GGTATGAAGGGCGAACGTCGTCGTGGCAAGGGTCA TGACGGCCTGTATCAAGGTCTGAGCACCGCGACCA AGGATACCTACGACGCGCTGCATATGCAGGCGCTG CCGCCGCGTTAA Signal NT WT 96 ATGTCTTGGAAAAAGGCTTTGCGGATCCCCGGAGG peptide HLA- CCTTCGGGCAGCAACTGTGACCTTGATGCTGTCGAT DQB1*02:01 GCTGAGCACCCCAGTGGCTGAGGGC 5' Flanking NT WT 9 CCACAACAA sequence HLA-DQ2- NT WT 27 CCTTTTCCACAGCCGGAACAACCATTT glia-Ω1 HLA-DQ2- NT WT 27 CCACAGCCGGAACAACCATTTCCCTGG glia-Ω2 Complete NT WT 33 CCTTTTCCACAGCCGGAACAACCATTTCCCTGG gliadin omega peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2- glia-Ω2) 3'Flanking NT WT 9 CAACCACAA sequence Linker 5xG NT WT 15 GGCGGCGGCGGCGGC 5' Flanking NT WT 9 CAACTTCAA sequence HLA-DQ2- NT WT 26 CCTTTTCCTCAACCTGAACTTCCTTA glia-α1a HLA-DQ2- NT WT 27 CCTCAACCTGAACTTCCTTATCCTCAA glia-α2 Complete NT WT 33 CCTTTTCCTCAACCTGAACTTCCTTATCCTCAA alpha gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) 3'Flanking NT WT 9 CCTCAACTT sequence Linker NT WT 51 GGCTCTGGATCTGGGTCCCTGGGATCTGGCTCTGG ATCTGGCTCTGGATCT HLA- NT WT 594 AGAGACTCTCCCGAGGATTTCGTGTACCAGTTTAAG DQB1*02:01 GGCATGTGCTACTTCACCAACGGGACAGAGCGCGT EC GCGTCTTGTGAGCAGAAGCATCTATAACCGAGAAG AGATCGTGCGCTTCGACAGCGACGTGGGGGAGTTC CGGGCGGTGACGCTGCTGGGGCTGCCTGCCGCCGA GTACTGGAACAGCCAGAAGGACATCCTGGAGAGGA AACGGGCGGCGGTGGACAGGGTGTGCAGACACAA CTACCAGTTGGAGCTCCGCACGACCTTGCAGCGGC GAGTGGAGCCCACAGTGACCATCTCCCCATCCAGG ACAGAGGCCCTCAACCACCACAACCTGCTGGTCTGC TCGGTGACAGATTTCTATCCAGCCCAGATCAAAGTC CGGTGGTTTCGGAATGACCAGGAGGAGACAGCTGG CGTTGTGTCCACCCCCCTTATTAGGAATGGTGACTG GACCTTCCAGATCCTGGTGATGCTGGAAATGACTCC CCAGCGTGGAGACGTCTACACCTGCCACGTGGAGC ACCCCAGCCTCCAGAGCCCCATCACCGTGGAGTGGC GGGCTCAATCTGAATCTGCCCAGAGCAAG CD28 TM NT WT 78 TTTTGGGTGCTGGTGGTGGTTGGGGGAGTCCTGGC TTGCTATAGCTTGCTAGTAACAGTGGCCTTTATTATT TTCTGG CD28 co- NT WT 126 GTGAGGAGTAAGAGGAGCAGGCTCCTGCACAGTG stimulatory ACTACATGAACATGACTCCCCGCCGCCCCGGGCCCA domain CCCGCAAGCATTACCAGCCCTATGCCCCACCACGCG ACTTCGCAGCCTATCGCTCC CD3 zeta NT WT 336 AGAGTGAAGTTCAGCAGGAGCGCAGACGCCCCCGC primary GTACCAGCAGGGCCAGAACCAGCTCTATAACGAGC signaling TCAATCTAGGACGAAGAGAGGAGTACGATGTTTTG domain GACAAGAGACGTGGCCGGGACCCTGAGATGGGGG GAAAGCCGAGAAGGAAGAACCCTCAGGAAGGCCT GTACAATGAACTGCAGAAAGATAAGATGGCGGAG GCCTACAGTGAGATTGGGATGAAAGGCGAGCGCCG GAGGGGCAAGGGGCACGATGGCCTTTACCAGGGTC TCAGTACAGCCACCAAGGACACCTACGACGCCCTTC ACATGCAGGCCCTGCCCCCTCGC Linker NT WT 9 GGCAGCGGC viral self- NT WT 57 GCCACCAACTTCAGCCTGCTGAAGCAGGCCGGCGA cleaving 2A CGTGGAGGAAAACCCTGGGCCC polypeptide Signal NT WT 69 ATGATCCTAAACAAAGCTCTGATGCTGGGGGCCCTT peptide HLA- GCCCTGACCACCGTGATGAGCCCCTGTGGAGGT DQA1*05:01 HLA- NT WT 591 GAAGACATTGTGGCTGACCACGTCGCCTCTTATGGT DQA1*05:01 GTAAACTTGTACCAGTCTTACGGTCCCTCTGGCCAG TACACCCATGAATTTGATGGAGATGAGCAGTTCTAC GTGGACCTGGGGAGGAAGGAGACTGTCTGGTGTTT GCCTGTTCTCAGACAATTTAGATTTGACCCGCAATTT GCACTGACAAACATCGCTGTCCTAAAACATAACTTG AACAGTCTGATTAAACGCTCCAACTCTACCGCTGCT ACCAATGAGGTTCCTGAGGTCACAGTGTTTTCCAAG TCTCCCGTGACACTGGGTCAGCCCAACATCCTCATCT GTCTTGTGGACAACATCTTTCCTCCTGTGGTCAACAT CACATGGCTGAGCAATGGGCACTCAGTCACAGAAG GTGTTTCTGAGACCAGCTTCCTCTCCAAGAGTGATC ATTCCTTCTTCAAGATCAGTTACCTCACCCTCCTCCCT TCTGCTGAGGAGAGTTATGACTGCAAGGTGGAGCA CTGGGGCCTGGACAAGCCTCTTCTGAAACACTGGG AGCCTGAGATTCCAGCCCCTATGTCAGAGCTCACAG AGACTGTGGTCTGC CD28 TM NT WT 78 TTTTGGGTGCTGGTGGTGGTTGGGGGAGTCCTGGC TTGCTATAGCTTGCTAGTAACAGTGGCCTTTATTATT TTCTGG CD28 co- NT WT 126 GTGAGGAGTAAGAGGAGCAGGCTCCTGCACAGTG stimulatory ACTACATGAACATGACTCCCCGCCGCCCCGGGCCCA domain CCCGCAAGCATTACCAGCCCTATGCCCCACCACGCG ACTTCGCAGCCTATCGCTCC CD3 zeta NT WT 336 AGAGTGAAGTTCAGCAGGAGCGCAGACGCCCCCGC primary GTACCAGCAGGGCCAGAACCAGCTCTATAACGAGC signaling TCAATCTAGGACGAAGAGAGGAGTACGATGTTTTG domain GACAAGAGACGTGGCCGGGACCCTGAGATGGGGG GAAAGCCGAGAAGGAAGAACCCTCAGGAAGGCCT GTACAATGAACTGCAGAAAGATAAGATGGCGGAG GCCTACAGTGAGATTGGGATGAAAGGCGAGCGCCG GAGGGGCAAGGGGCACGATGGCCTTTACCAGGGTC TCAGTACAGCCACCAAGGACACCTACGACGCCCTTC ACATGCAGGCCCTGCCCCCTCGC Stop NT WT 3 TGA CHAR_HLA- NT OPT 2667 ATGAGCTGGAAGAAAGCGCTGCGTATCCCGGGTGG DQ2.5-glia- CCTGCGTGCGGCGACCGTTACCCTGATGCTGAGCAT Ω1Ω2-glia- GCTGAGCACCCCGGTGGCGGAGGGTCCACAGCAGC α1α2 CCTTCCCTCAGCCAGAGCAGCCCTTTCCTTGGCAGC molecule (Ω- CCCAGGGCGGCGGCGGCGGCCAGCTGCAACCGTTT CCGCAGCCGGAACTGCCGTACCCGCAGCCGCAACT gliadin and GGGTAGCGGTAGCGGTAGCCTGGGCAGCGGCAGC α-gliadin) GGTAGCGGTAGCGGCAGCCGTGACAGCCCGGAGG ATTTCGTTTACCAATTCAAGGGCATGTGCTACTTCAC CAACGGCACCGAACGTGTGCGTCTGGTTAGCCGTA GCATCTACAACCGTGAGGAAATTGTGCGTTTCGACA GCGATGTTGGCGAGTTTCGTGCGGTGACCCTGCTG GGTCTGCCGGCGGCGGAGTACTGGAACAGCCAGAA GGACATCCTGGAACGTAAACGTGCGGCGGTGGATC GTGTTTGCCGTCACAACTATCAGCTGGAGCTGCGTA CCACCCTGCAACGTCGTGTGGAACCGACCGTTACCA TCAGCCCGAGCCGTACCGAAGCGCTGAACCACCAC AACCTGCTGGTGTGCAGCGTTACCGACTTCTACCCG GCGCAGATTAAAGTTCGTTGGTTTCGTAACGATCAA GAGGAAACCGCGGGTGTGGTTAGCACCCCGCTGAT CCGTAACGGCGACTGGACCTTCCAGATTCTGGTTAT GCTGGAGATGACCCCGCAACGTGGTGATGTGTACA CCTGCCACGTTGAACACCCGAGCCTGCAGAGCCCG ATTACCGTGGAGTGGCGTGCGCAGAGCGAAAGCGC GCAAAGCAAGTTTTGGGTTCTGGTGGTTGTGGGTG GCGTGCTGGCGTGCTACAGCCTGCTGGTGACCGTT GCGTTCATCATCTTCTGGGTGCGTAGCAAACGTAGC CGTCTGCTGCACAGCGACTATATGAACATGACCCCG CGTCGTCCGGGTCCGACCCGTAAGCACTACCAACCG TATGCGCCGCCGCGTGACTTTGCGGCGTACCGTAGC CGTGTTAAATTTAGCCGTAGCGCGGATGCGCCGGC GTACCAGCAGGGTCAGAACCAACTGTATAACGAGC TGAACCTGGGCCGTCGTGAGGAATATGACGTGCTG GATAAGCGTCGTGGTCGTGATCCGGAAATGGGTGG CAAGCCGCGTCGTAAAAACCCGCAGGAAGGTCTGT ACAACGAACTGCAAAAGGACAAAATGGCGGAGGC GTATAGCGAAATTGGTATGAAGGGCGAGCGTCGTC GTGGTAAAGGCCACGATGGTCTGTACCAGGGCCTG AGCACCGCGACCAAAGACACCTATGATGCGCTGCA CATGCAAGCGCTGCCGCCGCGTGGTAGCGGTGCGA CCAACTTCAGCCTGCTGAAGCAGGCGGGTGACGTT GAGGAAAACCCGGGCCCGATGATCCTGAACAAAGC GCTGATGCTGGGTGCGCTGGCGCTGACCACCGTTAT GAGCCCGTGCGGTGGCGAGGACATTGTGGCGGATC ACGTTGCGAGCTACGGCGTGAACCTGTACCAGAGC TATGGTCCGAGCGGCCAATACACCCACGAGTTCGAC GGTGATGAACAATTTTATGTTGACCTGGGCCGTAAG GAAACCGTGTGGTGCCTGCCGGTTCTGCGTCAGTTC CGTTTTGATCCGCAATTCGCGCTGACCAACATCGCG GTGCTGAAGCACAACCTGAACAGCCTGATTAAACGT AGCAACAGCACCGCGGCGACCAACGAGGTTCCGGA AGTGACCGTTTTCAGCAAAAGCCCGGTGACCCTGG GTCAGCCGAACATCCTGATTTGCCTGGTTGACAACA TCTTTCCGCCGGTTGTGAACATTACCTGGCTGAGCA ACGGTCACAGCGTGACCGAGGGCGTTAGCGAAACC AGCTTCCTGAGCAAGAGCGATCACAGCTTCTTTAAA ATCAGCTATCTGACCCTGCTGCCGAGCGCGGAGGA AAGCTATGACTGCAAGGTGGAGCACTGGGGTCTGG ATAAGCCGCTGCTGAAACACTGGGAGCCGGAAATT CCGGCGCCGATGAGCGAGCTGACCGAAACCGTTGT GTGCTTTTGGGTTCTGGTTGTGGTTGGTGGCGTGTT AGCTTGCTATAGCCTGCTGGTTACCGTGGCGTTTAT TATCTTCTGGGTTCGCAGCAAGCGTAGCCGTCTGCT GCATAGCGATTACATGAATATGACCCCGCGTCGTCC TGGCCCGACCCGCAAACATTATCAACCGTACGCGCC GCCGCGTGACTTTGCAGCGTATCGTAGCCGTGTTAA GTTTAGCCGTAGCGCGGACGCGCCGGCGTATCAAC AGGGCCAAAATCAGCTGTACAATGAACTGAATCTG GGTCGTCGTGAAGAGTACGATGTTCTGGACAAACG TCGTGGTCGTGACCCGGAGATGGGTGGCAAACCGC GTCGTAAGAACCCGCAGGAAGGTTTATATAATGAG CTGCAGAAAGATAAGATGGCGGAAGCGTATAGCGA AATCGGTATGAAGGGCGAACGTCGTCGTGGCAAGG GTCATGACGGCCTGTATCAAGGTCTGAGCACCGCG ACCAAGGATACCTACGACGCGCTGCATATGCAGGC GCTGCCGCCGCGTTAA Signal NT OPT 96 ATGAGCTGGAAGAAAGCGCTGCGTATCCCGGGTGG peptide HLA- CCTGCGTGCGGCGACCGTTACCCTGATGCTGAGCAT DQB1*02:01 GCTGAGCACCCCGGTGGCGGAGGGT 5' Flanking NT OPT 9 CCACAACAA sequence HLA-DQ2- NT OPT 27 CCTTTTCCACAGCCGGAACAACCATTT glia-Ω1 HLA-DQ2- NT OPT 27 CCACAGCCGGAACAACCATTTCCCTGG glia-Ω2 Complete NT OPT 33 CCTTTTCCACAGCCGGAACAACCATTTCCCTGG gliadin omega peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2- glia-Ω2) 3'Flanking NT OPT 9 CAACCACAA sequence Linker 5xG NT OPT 15 GGCGGCGGCGGCGGC 5' Flanking NT OPT 9 CAGCTGCAA sequence HLA-DQ2- NT OPT 27 CCGTTTCCGCAGCCGGAACTGCCGTAC glia-α1a HLA-DQ2- NT OPT 27 CCGCAGCCGGAACTGCCGTACCCGCAG glia-α2 Complete NT OPT 33 CCGTTTCCGCAGCCGGAACTGCCGTACCCGCAG alpha gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) 3'Flanking NT OPT 9 CCGCAACTG sequence Linker NT OPT 51 GGTAGCGGTAGCGGTAGCCTGGGCAGCGGCAGCG GTAGCGGTAGCGGCAGC HLA- NT OPT 594 CGTGACAGCCCGGAGGATTTCGTTTACCAATTCAAG DQB1*02:01 GGCATGTGCTACTTCACCAACGGCACCGAACGTGTG EC CGTCTGGTTAGCCGTAGCATCTACAACCGTGAGGAA ATTGTGCGTTTCGACAGCGATGTTGGCGAGTTTCGT GCGGTGACCCTGCTGGGTCTGCCGGCGGCGGAGTA CTGGAACAGCCAGAAGGACATCCTGGAACGTAAAC GTGCGGCGGTGGATCGTGTTTGCCGTCACAACTATC AGCTGGAGCTGCGTACCACCCTGCAACGTCGTGTG GAACCGACCGTTACCATCAGCCCGAGCCGTACCGA AGCGCTGAACCACCACAACCTGCTGGTGTGCAGCG TTACCGACTTCTACCCGGCGCAGATTAAAGTTCGTT GGTTTCGTAACGATCAAGAGGAAACCGCGGGTGTG GTTAGCACCCCGCTGATCCGTAACGGCGACTGGACC TTCCAGATTCTGGTTATGCTGGAGATGACCCCGCAA CGTGGTGATGTGTACACCTGCCACGTTGAACACCCG AGCCTGCAGAGCCCGATTACCGTGGAGTGGCGTGC GCAGAGCGAAAGCGCGCAAAGCAAG CD28 TM NT OPT 78 TTTTGGGTTCTGGTGGTTGTGGGTGGCGTGCTGGC GTGCTACAGCCTGCTGGTGACCGTTGCGTTCATCAT CTTCTGG CD28 co- NT OPT 126 GTGCGTAGCAAACGTAGCCGTCTGCTGCACAGCGA stimulatory CTATATGAACATGACCCCGCGTCGTCCGGGTCCGAC domain CCGTAAGCACTACCAACCGTATGCGCCGCCGCGTGA CTTTGCGGCGTACCGTAGC CD3 zeta NT OPT 336 CGTGTTAAATTTAGCCGTAGCGCGGATGCGCCGGC primary GTACCAGCAGGGTCAGAACCAACTGTATAACGAGC signaling TGAACCTGGGCCGTCGTGAGGAATATGACGTGCTG domain GATAAGCGTCGTGGTCGTGATCCGGAAATGGGTGG CAAGCCGCGTCGTAAAAACCCGCAGGAAGGTCTGT ACAACGAACTGCAAAAGGACAAAATGGCGGAGGC GTATAGCGAAATTGGTATGAAGGGCGAGCGTCGTC GTGGTAAAGGCCACGATGGTCTGTACCAGGGCCTG AGCACCGCGACCAAAGACACCTATGATGCGCTGCA CATGCAAGCGCTGCCGCCGCGT Linker NT OPT 9 GGTAGCGGT viral self- NT OPT 57 GCGACCAACTTCAGCCTGCTGAAGCAGGCGGGTGA cleaving 2A CGTTGAGGAAAACCCGGGCCCG polypeptide Signal NT OPT 69 ATGATCCTGAACAAAGCGCTGATGCTGGGTGCGCT peptide HLA- GGCGCTGACCACCGTTATGAGCCCGTGCGGTGGC DQA1*05:01 HLA- NT OPT 591 GAGGACATTGTGGCGGATCACGTTGCGAGCTACGG DQA1*05:01 CGTGAACCTGTACCAGAGCTATGGTCCGAGCGGCC AATACACCCACGAGTTCGACGGTGATGAACAATTTT ATGTTGACCTGGGCCGTAAGGAAACCGTGTGGTGC CTGCCGGTTCTGCGTCAGTTCCGTTTTGATCCGCAAT TCGCGCTGACCAACATCGCGGTGCTGAAGCACAAC CTGAACAGCCTGATTAAACGTAGCAACAGCACCGC GGCGACCAACGAGGTTCCGGAAGTGACCGTTTTCA GCAAAAGCCCGGTGACCCTGGGTCAGCCGAACATC CTGATTTGCCTGGTTGACAACATCTTTCCGCCGGTT GTGAACATTACCTGGCTGAGCAACGGTCACAGCGT GACCGAGGGCGTTAGCGAAACCAGCTTCCTGAGCA AGAGCGATCACAGCTTCTTTAAAATCAGCTATCTGA CCCTGCTGCCGAGCGCGGAGGAAAGCTATGACTGC AAGGTGGAGCACTGGGGTCTGGATAAGCCGCTGCT GAAACACTGGGAGCCGGAAATTCCGGCGCCGATGA GCGAGCTGACCGAAACCGTTGTGTGC 9 CD28 TM NT OPT 78 TTTTGGGTTCTGGTTGTGGTTGGTGGCGTGTTAGCT TGCTATAGCCTGCTGGTTACCGTGGCGTTTATTATCT TCTGG 0 CD28 co- NT OPT 126 GTTCGCAGCAAGCGTAGCCGTCTGCTGCATAGCGAT stimulatory TACATGAATATGACCCCGCGTCGTCCTGGCCCGACC domain CGCAAACATTATCAACCGTACGCGCCGCCGCGTGAC TTTGCAGCGTATCGTAGC 1 CD3 zeta NT OPT 336 CGTGTTAAGTTTAGCCGTAGCGCGGACGCGCCGGC primary GTATCAACAGGGCCAAAATCAGCTGTACAATGAACT signaling GAATCTGGGTCGTCGTGAAGAGTACGATGTTCTGG domain ACAAACGTCGTGGTCGTGACCCGGAGATGGGTGGC AAACCGCGTCGTAAGAACCCGCAGGAAGGTTTATA TAATGAGCTGCAGAAAGATAAGATGGCGGAAGCGT ATAGCGAAATCGGTATGAAGGGCGAACGTCGTCGT GGCAAGGGTCATGACGGCCTGTATCAAGGTCTGAG CACCGCGACCAAGGATACCTACGACGCGCTGCATAT GCAGGCGCTGCCGCCGCGT Stop NT OPT 3 TAA Table 4: Additional Sequences SEQ ID CHAR Amino Acid (AA), Length Sequence NO POLYPEPTIDE Nucleotide (NT) or Nucleotide Codon Optimised (NT OPT) 61 HLA-DQ8- AA 9 EGSFQPSQE glia-α1 62 CLIP peptide NT 28 CCGCTGCTGATGCAGGCGCTGCCGATG 3 Complete AA 14 QLQPFPQPELPYPQ alpha gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) with 5’ flanking 64 Complete AA 17 QLQPFPQPELPYPQPQL alpha gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) with 5’ flanking and 3’ flanking Complete AA 14 PFPQPELPYPQPQL alpha gliadin peptide (HLA-DQ2- glia-α1a and HLA-DQ2- glia-α2) with 3’ flanking Complete AA 14 PQQPFPQPEQPFPW gliadin omega peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2- glia-Ω2) with 5’ flanking Complete AA 17 PQQPFPQPEQPFPWQPQ gliadin omega peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2- glia-Ω2) with 5’ flanking and 3’ flanking Complete AA 14 PFPQPEQPFPWQPQ gliadin omega peptide (HLA-DQ2- glia-Ω1 and HLA-DQ2- glia-Ω2) with 3’ flanking HLA-DQ2- AA PYPQPELPY glia-α1b Complete AA PYPQPELPYPQ gliadin alpha peptide (HLA-DQ2- glia-α1b and HLA-DQ2- glia-α2) 71 Complete QLQPYPQPELPYPQ alpha gliadin peptide (HLA-DQ2- glia-α1b and HLA-DQ2- glia-α2) with 5’ flanking 72 Complete QLQPYPQPELPYPQPQL alpha gliadin peptide (HLA-DQ2- glia-α1b and HLA-DQ2- glia-α2) with 5’ flanking and 3’ flanking 73 Complete PYPQPELPYPQPQL alpha gliadin peptide (HLA-DQ2- glia-α1b and HLA-DQ2- glia-α2) with 3’ flanking Table 5: HLA-DQ8-glia CHAR molecule (#1) SEQ ID CHAR AA or NT Length Sequence NO POLYPEPTID E 74 CHAR_DQ8_ AA 861 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEGPSGE Celiac_pepti GSFQPSQENPQGSGSGSLGSGSGSGSGSRDSPEDFV de (a-gliadin) YQFKGMCYFTNGTERVRLVTRYIYNREEYARFDSDVG 2x CD28- VYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRH CD3z FL NYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSV TDFYPAQIKVRWFRNDQEETTGVVSTPLIRNGDWTF QILVMLEMTPQRGDVYTCHVEHPSLQNPIIVEWRAQ SESAQSKFWVLVVVGGVLACYSLLVTVAFIIFWVRSKR SRLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYR SRVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVL DKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEA YSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRGSGATNFSLLKQAGDVEENPGPMILNKALM LGALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPS GQYSHEFDGDEEFYVDLERKETVWQLPLFRRFRRFDP QFALTNIAVLKHNLNIVIKRSNSTAATNEVPEVTVFSKS PVTLGQPNTLICLVDNIFPPVVNITWLSNGHSVTEGVS ETSFLSKSDHSFFKISYLTFLPSADEIYDCKVEHWGLDE PLLKHWEPEIPTPMSELTEFWVLVVVGGVLACYSLLV TVAFIIFWVRSKRSRLLHSDYMNMTPRRPGPTRKHY QPYAPPRDFAAYRSRVKFSRSADAPAYQQGQNQLYN ELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGL YNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGL STATKDTYDALHMQALPPR Signal AA 32 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEG peptide DQB1*03:02: 01 5'Flanking AA 3 PSG 3aa DQ8 a- AA 9 EGSFQPSQE gliadin peptide 3'Flanking AA 3 NPQ 3aa Linker AA 17 GSGSGSLGSGSGSGSGS DQB1*03:02: AA 198 RDSPEDFVYQFKGMCYFTNGTERVRLVTRYIYNREEY 01 EC ARFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRA ELDTVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNH HNLLVCSVTDFYPAQIKVRWFRNDQEETTGVVSTPLI RNGDWTFQILVMLEMTPQRGDVYTCHVEHPSLQNP IIVEWRAQSESAQSK CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW CD28 IC (co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain) CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRGSG Linker AA 3 GSG P2A Opt AA 19 ATNFSLLKQAGDVEENPGP Signal AA 23 MILNKALMLGALALTTVMSPCGG peptide DQA1 DQA1*03:01: AA 194 EDIVADHVASYGVNLYQSYGPSGQYSHEFDGDEEFYV 01 EC DLERKETVWQLPLFRRFRRFDPQFALTNIAVLKHNLNI VIKRSNSTAATNEVPEVTVFSKSPVTLGQPNTLICLVD NIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKIS YLTFLPSADEIYDCKVEHWGLDEPLLKHWEPEIPTPM SELTE CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW 9 CD28 IC (co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain) 10 CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRStop AA 1 * Table 6: HLA-DQ8-glia CHAR molecule (#2) SEQ ID CHAR AA or NT Length Sequence NO POLYPEPTID E 78 CHAR_DQ8_ AA 712 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEGPSGE Celiac_pepti GSFQPSQENPQGSGSGSLGSGSGSGSGSRDSPEDFV de (a-gliadin) YQFKGMCYFTNGTERVRLVTRYIYNREEYARFDSDVG 2x CD28- VYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRH CD3z FL NYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSV TDFYPAQIKVRWFRNDQEETTGVVSTPLIRNGDWTF QILVMLEMTPQRGDVYTCHVEHPSLQNPIIVEWRAQ SESAQSKFWVLVVVGGVLACYSLLVTVAFIIFWVRSKR SRLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYR SRVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVL DKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEA YSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRGSGATNFSLLKQAGDVEENPGPMILNKALM LGALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPS GQYSHEFDGDEEFYVDLERKETVWQLPLFRRFRRFDP QFALTNIAVLKHNLNIVIKRSNSTAATNEVPEVTVFSKS PVTLGQPNTLICLVDNIFPPVVNITWLSNGHSVTEGVS ETSFLSKSDHSFFKISYLTFLPSADEIYDCKVEHWGLDE PLLKHWEPEIPTPMSELTEFWVLVVVGGVLACYSLLV TVAFIIFWVRSKR 75 Signal AA 32 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEG peptide DQB1*03:02: 01 5'Flanking AA 3 PSG 3aa 61 DQ8 a- AA 9 EGSFQPSQE gliadin peptide 3'Flanking AA 3 NPQ 3aa 6 Linker AA 17 GSGSGSLGSGSGSGSGS 76 DQB1*03:02: AA 198 RDSPEDFVYQFKGMCYFTNGTERVRLVTRYIYNREEY 01 EC ARFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRA ELDTVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNH HNLLVCSVTDFYPAQIKVRWFRNDQEETTGVVSTPLI RNGDWTFQILVMLEMTPQRGDVYTCHVEHPSLQNP IIVEWRAQSESAQSK 8 CD28 TM AA 26 FWVLVVVGGVLACYSLLVTVAFIIFW 9 CD28 IC (co- AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD stimulatory FAAYRS domain) 10 CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRGSG Linker AA 3 GSG 11 P2A Opt AA 19 ATNFSLLKQAGDVEENPGP 12 Signal AA 23 MILNKALMLGALALTTVMSPCGG peptide DQA1 77 DQA1*03:01: AA 194 EDIVADHVASYGVNLYQSYGPSGQYSHEFDGDEEFYV 01 EC DLERKETVWQLPLFRRFRRFDPQFALTNIAVLKHNLNI VIKRSNSTAATNEVPEVTVFSKSPVTLGQPNTLICLVD NIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKIS YLTFLPSADEIYDCKVEHWGLDEPLLKHWEPEIPTPMS ELTE 79 CD28 TM + AA 31 FWVLVVVGGVLACYSLLVTVAFIIFWVRSKR 5aa Stop AA 1 * Table 7: HLA-DQ8-glia CHAR molecule (#3) SEQ ID CHAR AA or NT Length Sequence NO POLYPEPTI DE 80 CHAR_DQ8 AA 863 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEGPSGE _Celiac_pe GSFQPSQENPQGSGSGSLGSGSGSGSGSRDSPEDFV ptide (a- YQFKGMCYFTNGTERVRLVTRYIYNREEYARFDSDVG gliadin) 2x VYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRH HLA TM+IC NYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSV 5aa extra + TDFYPAQIKVRWFRNDQEETTGVVSTPLIRNGDWTF 28IC-CD3z QILVMLEMTPQRGDVYTCHVEHPSLQNPIIVEWRAQ FL SESAQSKMLSGIGGFVLGLIFLGLGLIIHHRSQVRSKRS RLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRGSGATNFSLLKQAGDVEENPGPMILNKALM LGALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPS GQYSHEFDGDEEFYVDLERKETVWQLPLFRRFRRFDP QFALTNIAVLKHNLNIVIKRSNSTAATNEVPEVTVFSKS PVTLGQPNTLICLVDNIFPPVVNITWLSNGHSVTEGVS ETSFLSKSDHSFFKISYLTFLPSADEIYDCKVEHWGLDE PLLKHWEPEIPTPMSELTETVVCALGLSVGLVGIVVGT VLIIRGLRSVRSKRSRLLHSDYMNMTPRRPGPTRKHY QPYAPPRDFAAYRSRVKFSRSADAPAYQQGQNQLYN ELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGL YNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGL STATKDTYDALHMQALPPR Signal AA 32 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEG peptide DQB1*03:0 2:01 5'Flanking AA 3 PSG 3aa DQ8 a- AA 9 EGSFQPSQE gliadin peptide 3'Flanking AA 3 NPQ 3aa Linker AA 17 GSGSGSLGSGSGSGSGS DQB1*03:0 AA 198 RDSPEDFVYQFKGMCYFTNGTERVRLVTRYIYNREEY 2:01 EC ARFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRA ELDTVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNH HNLLVCSVTDFYPAQIKVRWFRNDQEETTGVVSTPLI RNGDWTFQILVMLEMTPQRGDVYTCHVEHPSLQNP IIVEWRAQSESAQSK DQB1*03:0 AA 26 MLSGIGGFVLGLIFLGLGLIIHHRSQ 2:01 TM + 5aa CD28 IC AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD (co- FAAYRS stimulatory domain) CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRGSG Linker AA 3 GSG P2A Opt AA 19 ATNFSLLKQAGDVEENPGP Signal AA 23 MILNKALMLGALALTTVMSPCGG peptide DQA1 DQA1*03:0 AA 194 EDIVADHVASYGVNLYQSYGPSGQYSHEFDGDEEFYV 1:01 EC DLERKETVWQLPLFRRFRRFDPQFALTNIAVLKHNLNI VIKRSNSTAATNEVPEVTVFSKSPVTLGQPNTLICLVD NIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKIS YLTFLPSADEIYDCKVEHWGLDEPLLKHWEPEIPTPMS ELTE 82 DQA1*03:0 AA 28 TVVCALGLSVGLVGIVVGTVLIIRGLRS 1:01 TM + 5aa 9 CD28 IC AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD (co- FAAYRS stimulatory domain) 10 CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRStop AA 1 * Table 8: HLA-DQ8-glia CHAR molecule (#4) SEQ ID CHAR AA or NT Length Sequence NO POLYPEPTI DE 83 CHAR_DQ8 AA 709 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEGPSGE _Celiac_pe GSFQPSQENPQGSGSGSLGSGSGSGSGSRDSPEDFV ptide (a- YQFKGMCYFTNGTERVRLVTRYIYNREEYARFDSDVG gliadin) VYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRH HLA DQ8 NYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSV HLA TM, TDFYPAQIKVRWFRNDQEETTGVVSTPLIRNGDWTF aan b +5aa QILVMLEMTPQRGDVYTCHVEHPSLQNPIIVEWRAQ extra HLA- SESAQSKMLSGIGGFVLGLIFLGLGLIIHHRSQVRSKRS IC + 1x 28- RLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS 3z, +IC 5aa RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD extra FL KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRGSGATNFSLLKQAGDVEENPGPMILNKALM LGALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPS GQYSHEFDGDEEFYVDLERKETVWQLPLFRRFRRFDP QFALTNIAVLKHNLNIVIKRSNSTAATNEVPEVTVFSKS PVTLGQPNTLICLVDNIFPPVVNITWLSNGHSVTEGVS ETSFLSKSDHSFFKISYLTFLPSADEIYDCKVEHWGLDE PLLKHWEPEIPTPMSELTETVVCALGLSVGLVGIVVGT VLIIRGLRS 75 Signal AA 32 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEG peptide DQB1*03:0 2:01 5'Flanking AA 3 PSG 3aa 61 DQ8 a- AA 9 EGSFQPSQE gliadin peptide 3'Flanking AA 3 NPQ 3aa 6 Linker AA 17 GSGSGSLGSGSGSGSGS 76 DQB1*03:0 AA 198 RDSPEDFVYQFKGMCYFTNGTERVRLVTRYIYNREEY 2:01 EC ARFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRA ELDTVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNH HNLLVCSVTDFYPAQIKVRWFRNDQEETTGVVSTPLI RNGDWTFQILVMLEMTPQRGDVYTCHVEHPSLQNP IIVEWRAQSESAQSK 81 DQB1*03:0 AA 26 MLSGIGGFVLGLIFLGLGLIIHHRSQ 2:01 TM + 5aa 9 CD28 IC AA 42 VRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRD (co- FAAYRS stimulatory domain) 10 CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPRGSG Linker AA 3 GSG 11 P2A Opt AA 19 ATNFSLLKQAGDVEENPGP 12 Signal AA 23 MILNKALMLGALALTTVMSPCGG peptide DQA1 77 DQA1*03:0 AA 194 EDIVADHVASYGVNLYQSYGPSGQYSHEFDGDEEFYV 1:01 EC DLERKETVWQLPLFRRFRRFDPQFALTNIAVLKHNLNI VIKRSNSTAATNEVPEVTVFSKSPVTLGQPNTLICLVD NIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKIS YLTFLPSADEIYDCKVEHWGLDEPLLKHWEPEIPTPMS ELTE 82 DQA1*03:0 AA 28 TVVCALGLSVGLVGIVVGTVLIIRGLRS 1:01 TM + 5aa Stop AA 1 * Table 9: HLA-DQ8-glia CHAR molecule (#5 / 6) SEQ ID CHAR AA or NT Length Sequence NO POLYPEPTI DE CHAR_DQ8 AA 709 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEGPSGE _Celiac_pe GSFQPSQENPQGSGSGSLGSGSGSGSGSRDSPEDFV ptide (a- YQFKGMCYFTNGTERVRLVTRYIYNREEYARFDSDVG gliadin) VYRAVTPLGPPAAEYWNSQKEVLERTRAELDTVCRH HLA DQ8 NYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSV HLA TM, TDFYPAQIKVRWFRNDQEETTGVVSTPLIRNGDWTF aan b+a QILVMLEMTPQRGDVYTCHVEHPSLQNPIIVEWRAQ +5aa extra SESAQSKMLSGIGGFVLGLIFLGLGLIIHHRSQKRGRKK HLA-IC, aan LLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCELRV b + 1x KFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKR 41BB- 3z FL RGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEI GMKGERRRGKGHDGLYQGLSTATKDTYDALHMQAL PPRGSGATNFSLLKQAGDVEENPGPMILNKALMLGA LALTTVMSPCGGEDIVADHVASYGVNLYQSYGPSGQ YSHEFDGDEEFYVDLERKETVWQLPLFRRFRRFDPQF ALTNIAVLKHNLNIVIKRSNSTAATNEVPEVTVFSKSPV TLGQPNTLICLVDNIFPPVVNITWLSNGHSVTEGVSET SFLSKSDHSFFKISYLTFLPSADEIYDCKVEHWGLDEPL LKHWEPEIPTPMSELTETVVCALGLSVGLVGIVVGTVL IIRGLRS Signal AA 32 MSWKKALRIPGGLRVATVTLMLAMLSTPVAEG peptide DQB1*03:0 2:01 5'Flanking AA 3 PSG 3aa DQ8 a- AA 9 EGSFQPSQE gliadin peptide 3'Flanking AA 3 NPQ 3aa Linker AA 17 GSGSGSLGSGSGSGSGS DQB1*03:0 AA 198 RDSPEDFVYQFKGMCYFTNGTERVRLVTRYIYNREEY 2:01 EC ARFDSDVGVYRAVTPLGPPAAEYWNSQKEVLERTRA ELDTVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNH HNLLVCSVTDFYPAQIKVRWFRNDQEETTGVVSTPLI RNGDWTFQILVMLEMTPQRGDVYTCHVEHPSLQNP IIVEWRAQSESAQSK DQB1*03:0 AA 26 MLSGIGGFVLGLIFLGLGLIIHHRSQ 2:01 TM + 5aa 41BB AA 42 KRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEE GGCEL CD3 zeta AA 112 RVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLD KRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAY SEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHM QALPPR GSG Linker AA 3 GSG P2A Opt AA 19 ATNFSLLKQAGDVEENPGP Signal AA 23 MILNKALMLGALALTTVMSPCGG peptide DQA1 DQA1*03:0 AA 194 EDIVADHVASYGVNLYQSYGPSGQYSHEFDGDEEFYV 1:01 EC DLERKETVWQLPLFRRFRRFDPQFALTNIAVLKHNLNI VIKRSNSTAATNEVPEVTVFSKSPVTLGQPNTLICLVD NIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKIS YLTFLPSADEIYDCKVEHWGLDEPLLKHWEPEIPTPMS ELTE DQA1*03:0 AA 28 TVVCALGLSVGLVGIVVGTVLIIRGLRS 1:01 TM + 5aa Stop AA 1 * References 1. Horn, P.A., et al., Highly efficient gene transfer into baboon marrow repopulating cells using GALV-pseudotype oncoretroviral vectors produced by human packaging cells. Blood, 2002.100(12): p.3960-3967. 2. Petersen, J., et al., T-cell receptor recognition of HLA-DQ2–gliadin complexes associated with celiac disease. Nature Structural & Molecular Biology, 2014. 21(5): p.480-488. 3. Vader, W., et al., The gluten response in children with celiac disease is directed toward multiple gliadin and glutenin peptides. Gastroenterology, 2002.122(7): p.1729-1737.

Claims

Claims 1. A chimeric HLA class II molecule comprising: (a) a first polypeptide comprising: (i) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain and (ii) a transmembrane domain; and (b) a second polypeptide comprising: (i) a second extracellular domain comprising an HLA-DQ α1α2 chain and (ii) a transmembrane domain wherein the first and / or second polypeptide further comprises (iii) an immune receptor intracellular signaling domain; wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively.

2. A fusion polypeptide, comprising, in an N-terminal to C-terminal orientation: (a) a first extracellular domain comprising a gluten-derived peptide comprising one or more gluten-derived epitopes and an HLA-DQ β1β2 chain; (b) a transmembrane domain; (c) a peptide cleavage signal; (d) a second extracellular domain comprising an HLA-DQ α1α2 chain; (e) a transmembrane domain; wherein the polypeptide further comprises an immune receptor intracellular signalling domain located at the C-terminus of (b) and / or (e), and wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; or wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively.

3. The fusion polypeptide of claim 2, further comprising an HLA-DQ β1β2 chain signal sequence located N-terminal to the first extracellular domain; and an HLA-DQ α1α2 chain signal sequence located N-terminal to the second extracellular domain.

4. The chimeric HLA class II molecule or the fusion polypeptide according to any one of the preceding claims, wherein the one or more gluten-derived epitopes are from a protein selected from the group consisting of: gliadin, glutenin, hordein, secalin and avenin.

5. The chimeric HLA class II molecule or the fusion polypeptide of claim 4, wherein the gliadin is alpha gliadin or omega gliadin.

6. The chimeric HLA class II molecule or the fusion polypeptide of claim 5, wherein the gliadin is alpha gliadin.

7. The chimeric HLA class II molecule or the fusion polypeptide of claim 6, wherein the one or more gluten-derived epitopes comprise the amino acid sequence of SEQ ID NO: 3, SEQ ID NO: 4, or SEQ ID NO:

69.

8. The chimeric HLA class II molecule or the fusion polypeptide of claim 6, wherein the one or more gluten-derived epitopes comprise the amino acid sequence of SEQ ID NO:

61.

9. The chimeric HLA class II molecule or the fusion polypeptide according to any one of the preceding claims, wherein the gluten-derived peptide comprises two or more gluten- derived epitopes.

10. The chimeric HLA class II molecule or the fusion polypeptide of claim 9, wherein the gluten-derived peptide comprises the amino acid sequences of SEQ ID NO: 3 and SEQ ID NO: 4; or SEQ ID NO: 69 and SEQ ID NO:

4.

11. The chimeric HLA class II molecule or the fusion polypeptide of claim 10, wherein the gluten-derived peptide comprises the amino acid sequence of SEQ ID NO: 5 or SEQ ID NO:

70.

12. The chimeric HLA class II molecule or the fusion polypeptide of claim 5, wherein the gliadin is omega gliadin.

13. The chimeric HLA class II molecule or the fusion polypeptide of claim 12, wherein the one or more gluten-derived epitopes comprise the amino acid sequence of SEQ ID NO: 44.

14. The chimeric HLA class II molecule or the fusion polypeptide of claim 12, wherein the one or more gluten-derived epitopes comprise the amino acid sequence of SEQ ID NO:

45.

15. The chimeric HLA class II molecule or the fusion polypeptide of claim 9, wherein the gluten-derived peptide comprises the amino acid sequence of SEQ ID NO: 44 and SEQ ID NO:

45.

16. The chimeric HLA class II molecule or the fusion polypeptide of claim 15, wherein the gluten-derived peptide comprises the amino acid sequence of SEQ ID NO:

46.

17. The chimeric HLA class II molecule or the fusion polypeptide according to any one of the preceding claims, wherein the gluten-derived peptide comprises four or more gluten- derived epitopes.

18. The chimeric HLA class II molecule or the fusion polypeptide of claim 17, wherein the gluten-derived peptides are selected from the group consisting of SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO: 69, SEQ ID NO: 44 and SEQ ID NO:

45.

19. The chimeric HLA class II molecule or the fusion polypeptide of claim 18, wherein the gluten-derived peptide comprises: (a) the amino acid sequence of SEQ ID NO: 5 and SEQ ID NO: 46, optionally wherein the gluten-derived peptide comprises a linker between the amino acid sequence of SEQ ID NO: 5 and SEQ ID NO: 46, or (b) the amino acid sequence of SEQ ID NO: 70 and SEQ ID NO: 46, optionally wherein the gluten-derived peptide comprises a linker between the amino acid sequence of SEQ ID NO: 70 and SEQ ID NO:

46.

20. The chimeric HLA class II molecule or the fusion polypeptide according to any one of the preceding claims, wherein the first extracellular domain further comprises a linker sequence between the gluten-derived peptide and the HLA-DQ β1β2 chain.

21. The chimeric HLA class II molecule or the fusion polypeptide according to any one of the preceding claims, wherein the gluten-derived peptide further comprises flanking amino acids at the N- and / or C- terminal side of the gluten-derived epitope, optionally wherein the flanking amino acids are natural flanking amino acids.

22. The chimeric HLA class II molecule or the fusion polypeptide according to any one of the preceding claims, wherein the transmembrane domain is selected from the group consisting of: alpha or beta chain of CD28, CD4, CD5, CD8, CD9, CD16, CD22, CD27, CD33, CD37, CD45, CD64, CD80, CD86, CD134, CD137, CD152, CD154, PD1, HLA-DR, HLA-DQ or HLA-DP.

23. The chimeric HLA class II molecule or the fusion polypeptide of claim 22, wherein the transmembrane domain is a CD28 or HLA-DQ transmembrane domain.

24. The chimeric HLA class II molecule or the fusion polypeptide according to any one of the preceding claims, wherein the immune receptor intracellular signalling domain comprises one or more co-stimulatory signalling domains.

25. The chimeric HLA class II molecule or the fusion polypeptide of claim 24, wherein the one or more co-stimulatory signalling domain is selected from the group consisting of: TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, TLR10, CARD11, CD2, CD7, CD27, CD28, CD30, CD40, CD54 (ICAM), CD83, CD134 (0X40), CD137 (4-1BB), CD154 (CD40L), CD278 (ICOS), DAP10, LAT, NKD2C, SLP76, TRIM, and ZAP70 co-stimulatory signalling domain.

26. The chimeric HLA class II molecule or the fusion polypeptide of claim 25, wherein the one or more co-stimulatory signalling domain is a CD28 or CD137 (4-1BB) co-stimulatory signalling domain.

27. The chimeric HLA class II molecule or the fusion polypeptide according to any one of the preceding claims, wherein the immune receptor intracellular signalling domain comprises a primary signalling domain.

28. The chimeric HLA class II molecule or the fusion polypeptide of claim 27, wherein the primary signalling domain is selected from the group consisting of: FcRγ, FcRβ, CD3γ, CD3δ, CD3ε, CD3ζ, CD22, CD79b, and CD66d.

29. The chimeric HLA class II molecule or the fusion polypeptide of claim 28, wherein the primary signalling domain is CD3ζ.

30. A nucleic acid encoding a chimeric HLA class II molecule, or a fusion polypeptide, according to any one of the preceding claims, optionally wherein the nucleic acid is RNA and / or DNA.

31. A vector comprising a nucleic acid according to claim 30.

32. A cell comprising one or more nucleic acid, vector, chimeric HLA class II molecule, and / or fusion polypeptide according to any one of the preceding claims.

33. The cell according to claim 32, wherein the cell is a T cell, optionally wherein the T cell is selected from the group consisting of a CD8+ T cell, an NK T cell, CD3+ T cell and γδ T cell, or a mixture of any one thereof.

34. The cell according to claim 33, wherein the cell is a NK cell or an innate lymphoid cell (ILC).

35. A cell comprising at least two of the following: a) a first nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide according to any one of the preceding claims, wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*05 and HLA-DQB1*02, respectively; b) a second nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide according to any one of the preceding claims, wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*02 and HLA-DQB1*02, respectively; and / or c) a third nucleic acid, vector, chimeric HLA class II molecule, or fusion polypeptide according to any one of the preceding claims, wherein the HLA-DQ α1α2 and β1β2 chains are encoded by the genes HLA-DQA1*03 and HLA-DQB1*03, respectively.

36. The cell according to claim 35, wherein the HLA-DQA1*02 and HLA-DQB1*02 are HLA-DQA1*02:01 and HLA-DQB1*02:02 respectively.

37. The cell according to claim 35 or 36, wherein the HLA-DQA1*05 and HLA-DQB1*02 are HLA-DQA1*05:01 and HLA-DQB1*02:01 respectively.

38. A composition comprising a nucleic acid, vector, chimeric HLA class II molecule, fusion polypeptide and / or cell according to any one of the preceding claims.

39. A pharmaceutical composition comprising a nucleic acid, vector, chimeric HLA class II molecule, fusion polypeptide and / or cell according to any one of the preceding claims.

40. A pharmaceutical composition according to claim 39, for use as a medicament.

41. A pharmaceutical composition according to claim 39, for use in treating or preventing celiac disease in a HLA-DQ positive subject.

42. The pharmaceutical composition for use, according to claim 41, wherein the subject is HLA-DQA1*02-HLA-DQB1*02, HLA-DQA1*05-HLA-DQB1*02, and / or a HLA-DQA1*03- DQB1*03 positive.

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