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Stig Tollefsen 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, Oslo, Norway.
Helene Arentz-Hansen 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, Oslo, Norway.
Burkhard Fleckenstein 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, Oslo, Norway.
Øyvind Molberg 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, Oslo, Norway.
Melinda Ráki 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, Oslo, Norway.
Kwok 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Are holland casino contact rotterdam fantasy)))) Center, Oslo, Norway.
Günther Jung 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, Oslo, Norway.
Lundin 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, Oslo, Norway.
Sollid 1Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, Oslo, Norway.
Address correspondence to: Ludvig M.
Sollid, Institute of Immunology, University of Oslo, Rikshospitalet-Radiumhospitalet Medical Center, N-0027 Oslo, Norway.
Phone: 47-230-73811; Fax: 47-230-73510; E-mail:.
Celiac disease is associated with HLA-DQ2 and, to a lesser extent, HLA-DQ8.
Type 1 diabetes is associated with the same DQ molecules in the dq8 casino strats order and with possible involvement of trans-encoded DQ heterodimers.
T cells that are reactive with gluten peptides deamidated by transglutaminase 2 and invariably restricted by DQ2 or DQ8 can be isolated from celiac lesions.
We used intestinal T cells from celiac patients to map DQ2 and DQ8 epitopes within 2 representative gluten proteins, α-gliadin and γ-gliadin.
For α-gliadin, DQ2- and DQ8-restricted T cells recognized deamidated peptides of 2 dq8 casino strats regions.
For γ-gliadin, DQ2- and DQ8-restricted T cells recognized deamidated peptides of the same region.
Peptides combining the DQ2 and DQ8 signatures could be presented by DQ2, DQ8, and trans-encoded DQ heterodimers.
Our findings shed light on the basis for the HLA associations in celiac disease and type 1 diabetes.
Introduction Celiac disease is a chronic disease of the small intestine caused by an inappropriate immune response to ingested wheat gluten proteins and related proteins in barley and rye .
The celiac lesion is characterized by villous atrophy, crypt hyperplasia, and a dense infiltration of lymphocytes in the epithelium and lamina propria.
A significant proportion of the genetic predisposition comes from MHC-linked HLA-linked genes, estimated to account for about 50% of the genetic load.
The strong HLA association implies a central role for CD4 + T click the following article in disease pathogenesis.
In fact, CD4 + gluten-specific T cells can be readily isolated from small intestinal biopsies of celiac patients, but not from healthy controls .
Strikingly, these T cells are exclusively restricted by the DQ2 or DQ8 molecules, strongly indicating that the DQ2 and DQ8 molecules are important peptide-presenting molecules in this disease.
The great majority of the gluten-specific T cells recognize gluten only — or better — after the gluten antigen has been modified by transglutaminase 2 TG2 .
This enzyme catalyzes an ordered deamidation of certain glutamine residues by converting them to glutamate residues.
Both DQ2 and DQ8 have preferences for binding of peptide ligands with multiple negatively charged residues —.
Several epitopes have been identified, and much has been learned about T cell epitopes recognized by DQ2-restricted T cells — ; conversely, our understanding of DQ8-restricted gluten T cell epitopes is more limited, as only 2 epitopes have been identified so far .
Commonly, all the DQ2- and DQ8-restricted intestinal T cell epitopes have been defined from T cells that are derived from intact celiac lesion biopsies stimulated ex vivo with enzymatically digested i.
The main effect of performing such an ex vivo antigen challenge is to enrich for T cells specific for the challenging antigen.
Thus the possibility cannot be excluded that the enzymatic pretreatment of the gluten antigen introduces a bias by limiting the number of gluten peptide sequences available for in situ activation of the T impossible employment in casino nsw simply within the biopsy specimen.
To ensure an unbiased representation of gluten peptides, we established a number of independent T cell lines from biopsies challenged with a digest of whole gluten, with a digest of a recombinant gliadin protein α-gliadinand with overlapping peptides spanning the whole sequence of the same recombinant protein.
Having confirmed the methods to give full representation of the epitopes, we proceeded to compare the reactivity patterns of T cell lines of celiac disease patients with different HLA types to 2 prototype gliadins α-gliadin and γ-gliadin.
Interestingly, DQ2 and DQ8 employed different rules for selection of epitopes for T cell presentation.
We identified 2 γ-gliadin peptides recognized in the same binding register when presented by DQ2 or DQ8 molecules, but the requirement for glutamine residues to be deamidated by TG2 differed between the DQ2-restricted and the DQ8-restricted T cells.
These findings further increase our understanding of the molecular basis for HLA association in celiac disease.
Moreover, the results are relevant for type 1 diabetes.
In contrast to celiac disease, the antigen eliciting type 1 diabetes is as yet unidentified.
Thus the rules dictating T cell recognition of dq8 casino strats peptides in the context of DQ2 and DQ8 can provide clues to understand the hallmarks of antigenic peptide s that can elicit type 1 diabete.
In vitro challenge of biopsies derived from celiac disease patients with different gluten antigens gives the same T cell response pattern.
To test whether the enzymatic treatment of gluten antigen, which was used to stimulate the biopsies, affected epitope mapping and introduced an artificial bias to the confinement of epitopes to proline-rich regions, we first compared the specificity of T cell lines isolated from biopsies stimulated in parallel with chymotrypsin-digested natural gluten, chymotrypsin-digested recombinant α-gliadin, or a panel of overlapping peptides covering the same α-gliadin.
Multiple intestinal biopsy specimens were obtained from 7 celiac disease patients 4 DQ2 +DQ8 —, 2 DQ2 +DQ8 +, and 1 DQ2 —DQ8 + and stimulated with distinct antigens.
From each biopsy, 4 polyclonal T cell lines were generated.
Gluten-reactive T cell lines were expanded for 2 weeks and tested against the panel of TG2-treated overlapping peptides of α-gliadin.
Parallel T cell lines derived from biopsies stimulated with chymotrypsin-treated gluten, chymotrypsin-treated recombinant α-gliadin, and overlapping α-gliadin peptides were obtained from 4 of the patients.
From the rest of the patients we obtained T cell lines that were derived from biopsies stimulated with 2 of the 3 antigens.
In all cases we found that T cell lines isolated from parallel biopsy specimens stimulated either with chymotrypsin-treated recombinant α-gliadin or overlapping α-gliadin peptides had nearly identical recognition patterns when tested against the peptide panel Tables and and Figure.
The same recognition pattern was also seen for 8 different T cell lines isolated from biopsy specimens stimulated with chymotrypsin-treated gluten Table.
In some cases we found that the maximum response of these latter lines was lower than the maximum response of the T cell lines derived from biopsies stimulated with recombinant gliadin or check this out peptides Figure.
This may reflect the lower concentration of each of the α-gliadin peptides in the whole gluten mixture.
In essence, the reactivity patterns of the resulting T cell lines were superimposable regardless of which form of antigen was initially used to stimulate the biopsies.
Testing of T cell lines TCL isolated from biopsy specimens of a DQ2 + DQ8 + patient CD465 stimulated in parallel with A chymotrypsin-treated gluten, B chymotrypsin-treated recombinant AJ133612 α-gliadin, and C overlapping AJ133612 α-gliadin peptides against the whole panel of TG2-treated AJ133612 α-gliadin peptides 1409—1457.
TG2-treated gluten and TG2-treated recombinant AJ133612 α-gliadin were used as positive controls.
Responses are given as the stimulation index.
Amino acid sequences of the peptides in AJ133612 α-gliadin and M36999 γ-gliadin that elicited a positive T cell response T cell responses to TG2-treated, overlapping AJ133612 α-gliadin peptides in intestinal T cell lines derived from 9 adult CD patients DQ2- and DQ8-restricted T cells recognize peptides in different regions of α-gliadin.
Interestingly, we found that the DQ2-restricted T cell responses and the DQ8-restricted T cell responses were localized to 2 separate regions of α-gliadin regions 1 and 2; Figure and Table.
T cell lines from patients carrying DQ2 or DQ8 were tested against the TG2-treated α-gliadin peptides with APCs homozygous for DQ2 or DQ8, respectively.
In experiments with T cell lines derived from DQ2 +DQ8 + heterozygous patients, the α-gliadin peptides were tested for recognition using APCs expressing either DQ2 or DQ8.
We found that almost all the DQ2-restricted T cell responses in T cell lines derived from the DQ2 +DQ8 — and DQ2 +DQ8 + patients were directed toward peptides within the 33-mer peptide fragment in the N-terminal region of α-gliadin region 1.
The DQ8-restricted T cell response of T cell lines obtained from the DQ2 —DQ8 + patients and 1 of the DQ2 +DQ8 + patients only recognized peptides located in the C-terminal region region 2; Table.
The only exception to this pattern was seen in 1 DQ2 +DQ8 — T cell line patient CD510 derived from a biopsy stimulated with overlapping α-gliadin peptides, which had a weak response to a peptide in region 2 stimulation index of 5 compared with the maximum response of 59 toward peptides 1421—1422 within region 1; see Table.
T cell lines derived from biopsy specimens of 3 different patients stimulated with chymotrypsin-treated recombinant AJ133612 α-gliadin were tested against the panel of TG2-treated AJ133612 α-gliadin peptides as in Figure.
Patient CD506 is DQ2 +DQ8 — Apatient CD559 is DQ2 +DQ8 + Band patient CD489 is DQ2 —DQ8 + C.
TG2-treated gluten and TG2-treated recombinant AJ133612 α-gliadin were used as positive controls.
Black bars CD114 cells as APCs indicate DQ2-restricted T cell responses, and white bars 9092 cells as APCs indicate DQ8-restricted responses.
By cloning 2 of the α-gliadin—reactive DQ8-restricted T cell lines, we obtained 2 T cell clones TCC489.
Both clones were found to be specific for the previously identified DQ8—α-I epitope .
Despite several attempts, we obtained no T cell clones reactive with peptides 1448 or 1450, to which some of the T cell lines were reactive Table.
Testing for T cell recognition of variants of the 228 SG QGSFQPSQQ NPQ 241 peptide of AJ133612 α-gliadin.
The peptide harbors the DQ8—α-I epitope.
Responses are shown as cpm × 10 3.
TG2-treated, native sequence treated with TG2, used as a control.
DQ2- and DQ8-restricted T cells recognize peptides in the same region of γ-gliadin.
Having validated a robust protocol for epitope mapping, we next sought to identify the epitopes that were recognized by DQ2- source DQ8-restricted T cells in γ-gliadin.
We subjected γ-gliadin to this analysis.
We tested T cell lines from 9 different celiac patients 2 DQ2 +DQ8 —, 4 DQ2 +DQ8 +, source 3 DQ2 —DQ8 +; Table.
The T cell lines were derived from biopsies stimulated with chymotrypsin-treated gluten in 7 patients or with overlapping γ-gliadin peptides in 3 patients; biopsies from 1 patient were treated in parallel with both types of antigens.
The T cell lines obtained were next tested against the panel of TG2-treated peptides Figure.
The recognition pattern of γ-gliadin resembled the recognition pattern of α-gliadin in that only peptides in the proline-rich regions were recognized and that T cell lines derived from biopsies stimulated with gluten or tiled γ-gliadin peptides mainly recognized the same individual peptides.
However, the response pattern toward γ-gliadin differed considerable from that of α-gliadin in the way that the DQ2- and DQ8-restricted responses were directed toward the peptides of the same region.
Moreover, a higher number of peptides were recognized of γ-gliadin than of α-gliadin Table.
Testing of T cell lines isolated from biopsy specimens of a DQ2 + DQ8 + patient CD548 stimulated in parallel with chymotrypsin-treated gluten A and overlapping M36999 γ-gliadin peptides B against the panel of TG2-treated M36999 peptides 1369—1527.
Peptides were tested at 10 μM.
TG2-treated gluten was used as a positive control.
Black CD114 cells as APCs and white bars 9092 cells as APCs indicate DQ2-restricted and DQ8-restricted T cell responses, respectively.
T cell responses to TG2-treated, overlapping M36999 γ-gliadin peptides in intestinal T cell https://eronline.ru/casino/monticello-casino-hours.html derived from 9 adult CD patients DQ8-restricted T cell epitopes of γ-gliadin.
In previous studies, several DQ2-restricted T cell epitopes have been mapped to the proline-rich region of γ-gliadin .
In order to identify and characterize DQ8-restricted epitopes, we cloned a T cell line of a DQ2 —DQ8 + patient that was responsive to several peptides of γ-gliadin in a TG2-dependent manner.
We obtained 2 T cell clones, TCC544.
These peptides share the sequence QQPQQPFPQ, which we identified to be the P1—P9 core of the epitopes recognized by either of the T cell clones data not shown.
DQ2- and DQ8-restricted T cells recognize the same γ-gliadin epitopes in identical registers but are sensitive to deamidation at different positions.
The QQPQQPFPQ sequence is the core part of the DQ2—γ-VII epitope previously found to be recognized by the DQ2-restricted T cell clone TCC387.
The 2 DQ8-restricted T cell clones, TCC544.
The DQ2-restricted clone, Dq8 casino strats />T cell recognition of variants of the 61 QFPQT QQPQQPFPQ PQQTFP 80 peptide of M36999 γ-gliadin.
The peptide harbors the DQ2—γ-VII and DQ8—γ-I epitopes.
Responses are shown as cpm × 103.
Electrospray ionization—mass spectrometry ESI-MS analysis of peptide 1375 revealed an average deamidation of 1.
For peptide 1378, a deamidation of 1.
These data suggest that the regional selectivity of TG2 for deamidation is influenced by residues flanking the core region of the T cell epitopes and that deamidation in position P1 is predominantly required for DQ8-restricted recognition of these peptides.
Interestingly, both peptides show only little deamidation in position P4, where deamidation is important for DQ2-restricted recognition.
The sequence QQPQQPFPQ is very similar to the sequence QQPQQPYPQ, which is the core region of the previously characterized DQ2—γ-III epitope found in γ-gliadin .
We thus tested the 2 T cell clones TCC544.
The DQ2—γ-III—reactive T cell clones TCC430.
The reactivity of the DQ2- and DQ8-restricted T cell clones to the fragment 66FPQQPQQPYPQQPQQ 80 of γ-gliadin is depicted in Figure.
T cell recognition of variants of the 66 FPQQPQQPYPQQPQQ 80 peptide of AJ416339 γ-gliadin.
The peptide harbors the DQ2—γ-III and DQ8—γ-I epitopes.
Responses are given in cpm × 103.
This peptide was also subjected to analysis by ESI-MS, which demonstrated an average deamidation of 1.
We found that the 2 DQ8-restricted clones TCC544.
Peptides singly substituted at 68 or 76 were equally well recognized by both clones.
Note that although they were derived from the same patients and had similar reactivity patterns, these 2 clones are not sister clones as they express different TCR Vβ chains TCC544.
In order to determine whether this DQ8-restricted recognition pattern was reflected in polyclonal T cell lines likely containing T cells with multiple specificities, we further tested the same peptides for recognition by the 2 T cell lines from which these clones were established patient CD544 and a third T cell line from another DQ8 + patient CD469.
By contrast, when testing the DQ2-restricted T cell clones TCC430.
In aggregate these results demonstrate that in some instances DQ2- and DQ8-restricted T cells recognize the same gliadin peptides in exactly the same registers, but the DQ2- and DQ8-restricted T cells have different requirements for deamidation.
T cell recognition of the same peptides in the same registers when bound to DQ2 and DQ8 prompted us to investigate whether trans-encoded heterodimers i.
The expression of HLA-DQ molecules by these cell dq8 casino strats was analyzed by flow cytometry Supplemental Figure 1; available online with this article; doi:10.
We tested the T cell clones TCC387.
In particular, the clone TCC387.
The T cell clone TCC544.
The T cell clones TCC430.
This may suggest that neither of the trans-encoded heterodimers is effective i presenting gluten epitopes with a proline residue at P1.
T cell recognition of peptides presented by cis- and trans- encoded DQ heterodimers.
A Recognition of variants of the 63PQT QQPQQPFPQPQ 76 peptide described in Figure by the T cell clone TCC387.
B Recognition of variants of the 66FP QQPQQPYPQQPQQ 80 peptide described in Figure by the T cell clone TCC544.
Discussion This study demonstrates that DQ2 and DQ8 have preference for binding peptides with negatively charged anchor residues, but that the 2 HLA molecules employed different criteria for selection of deamidated gluten T cell epitopes.
This can result in the selection of distinct epitopes localized in different regions of a gliadin protein, but it can also result in the selection of epitopes that combine the DQ2 and DQ8 signatures and are recognized in exactly the same binding register when bound to DQ2 or DQ8.
These findings further expand our understanding of the mechanisms underlying the HLA association in celiac disease.
The superimposable reactivity patterns toward the peptide panels of the T cell lines established by stimulation of biopsies with chymotrypsin-digested whole gluten, chymotrypsin-digested recombinant gliadin, or the collection of overlapping peptides indicate that there is no bias in our detection of epitopes.
In α-gliadin, the DQ2- and DQ8-restricted T cell responses were localized to 2 different regions of the protein regions 1 and 2.
This observation suggested that the DQ2 and DQ8 molecules select for different epitopes.
The overlapping recognition patterns more info γ-gliadin peptides by DQ2- and DQ8-restricted T cell lines were therefore surprising.
However, further analysis with T cell clones revealed that the DQ2- and DQ8-restricted T cells recognized different features of the γ-gliadin peptides.
We found DQ8-restricted T cell clones that were reactive to peptides harboring the sequence QQPQQPFPQ following TG2 treatment.
This sequence is expressed in 4 of the individual peptides, and reactivity to this epitope is a major contributor to the observed DQ8-associated reactivity pattern of the polyclonal T cell lines.
The QQPQQPFPQ sequence is identical to the core region of the previously characterized DQ2—γ-VII epitope.
The DQ2- and DQ8-restricted T cells recognized this peptide in the same register, but with different requirements for deamidation.
A similar sequence, QQPQQPYPQ, is found in another γ-gliadinand this is the core sequence of the previously characterized DQ2—γ-III epitope.
We found that the DQ8-restricted T cell clones also recognized TG2-treated peptides harboring this sequence.
Again the requirements for deamidation were casino everett boston to be different for the DQ2- and DQ8-restricted T cell clones, following the same pattern as for the QQPQQPFQ sequence.
The criteria employed by DQ2 and DQ8 molecules for selecting epitopes were seen from alignment of the core regions of DQ2- and DQ8-restricted gliadin epitopes Table.
Both DQ2 and DQ8 have a preference for binding of negatively charged residues.
For the DQ2-restricted gluten T cell epitopes, glutamate residues formed by TG2-mediated deamidation were found in P1, P4, P6, P7, and P9, but only deamidation in P4 and P6 — and, rarely, P7 — seem to be crucial for T cell recognition.
This preference for binding of negatively charged residues in the positions P1 and P9 is consistent with other studies of the DQ8 binding motif —.
It is striking that, for both DQ2- and DQ8-restricted T cells, it is deamidation at positions with presumed orientation of the side chains toward the MHC that affects T cell recognition.
Notably, the peptide binding preferences we observed for DQ8 and DQ2 are in accordance with the X-ray crystal structures of these molecules —.
DQ2 binds gluten peptides with the proline residues localized in P1, P3, P5, P6, and P8 but not in P2, P4, P7, or P9 .
This pattern is similar for DQ8, which bind peptides with proline residues in P3, P6, and P8 Table.
An important difference between DQ2 and DQ8, however, is at P1.
In most MHC class II molecules, including DQ8, there is a hydrogen bond between the amide nitrogen of the P1 residue and the backbone carbonyl of residue α53 .
This appears article source to be the case for DQ2.
The majority of the characterized DQ2-restricted gluten T cell epitopes have proline residues at P1.
The fact that DQ2 is better suited than DQ8 to bind the proline-rich gluten peptides that survive gastrointestinal digestion may be the reason why DQ2 is a stronger susceptibility determinant for celiac disease than DQ8.
In celiac disease, the major susceptibility factor is DQ2, whereas DQ8 adds a small risk independent of DQ2.
This has led to the hypothesis click trans-encoded dimers, i.
Which epitopes are involved in human type 1 diabetes and what characteristics they should have are basically unknown, although there are suggestions in the literature —including posttranslationally modified antigens.
There is no existing evidence for a role of TG2 in the pathogenesis of type 1 diabetes by deamidating antigens, although this possibility cannot be excluded either.
The molecular understanding of HLA association in celiac disease has made huge advances source recent years, much of it because of the identification of disease-relevant gluten cell epitopes.
A similar advance has not taken place for type 1 diabetes, and an obvious obstacle is the lack of knowledge of disease-relevant T cell epitopes; to define them is a major goal.
The gluten epitopes recognized by intestinal T cells of celiac disease patients are naturally selected by DQ2 and DQ8 and they are disease relevant.
Thus this model system has advantages over transgenic mouse systems, in which the T cell epitopes studied are often the result of forced immunization with the use of adjuvants.
The trans-encoded heterodimers can possibly present a unique peptide or set of peptides.
Alternatively, a peptide or limited set of peptides that could be presented by both DQ2 and DQ8 could be even more effectively presented by the trans-encoded heterodimers.
The findings of this study provide support for the latter model, as we demonstrated the existence of sequence-related peptides that bound to DQ2 and DQ8 in the same registers and did so by incorporating both the DQ2 and the DQ8 binding motifs.
We cannot exclude the possibility that this effect is mediated at the level of the TCR, and future work needs to corroborate this notion by peptide binding analysis.
Moreover, our testing of T cell recognition of peptides in the context of the trans-encoded heterodimers was suboptimal, as we used T cell clones that were screened and selected for their ability to recognize peptides in the context of encoded DQ2 or DQ8.
Our observations also raise the question of why there is no synergistic effect between DQ2 and DQ8 as predisposing elements in celiac disease.
In summary, this work give details of antigen presentation by DQ2 and DQ8 molecules that further expand the knowledge of the HLA association in celiac disease and allow us to predict essential features of peptides that are involved in type 1 diabetes.
Small intestinal biopsies were obtained by gastroduodenoscopy from 12 Norwegian adult celiac disease patients 4 were DQ2 +DQ8 —, 4 were DQ2 +DQ8 +, and 4 were DQ2 —DQ8 +.
All patients gave written informed consent before the gastroduodenoscopy.
The study received approval from the Regional Committee for Medical Research Ethics Ullevål University Hospital, Oslo, Norway.
The preparation and subsequent chymotrypsin treatment of gliadin, gluten, and recombinant α-gliadin were performed as described previously .
The overlapping α-gliadin peptides were made as pentadecapeptides overlapping with 10 amino acids.
To avoid the formation of disulphide bonds, all the cysteine residues were substituted with alanine.
The overlapping γ-gliadin peptide was made as eicosapeptides overlapping with 10 amino acids.
The amino acid sequence of gliadin peptides that elicited a positive T cell response are listed in Table.
The mouse mAbs 2.
Staining was done with unlabeled primary mAbs except for 2.
E11, which, in some instances, was used directly labeled with FITC.
As secondary antibodies for the mouse mAbs, we used FITC-conjugated Goat Anti-Mouse IgG or FITC-conjugated Goat Anti-Mouse IgG1 SouthernBiotech.
SFR20-DQα5 were detected by biotinylated Mouse Anti-Rat Fc-Ig antibody Accurate followed by Streptavidin-PE Invitrogen.
The HLA restriction of the T cells was determined by testing inhibition of T cell proliferation in the presence of purified mAb B8.
Flow cytometry and cell sorting.
Expression of HLA-DQ molecules was analyzed by a FACSCalibur instrument with CellQuest software version 4.
Cell sorting was performed with a FACSAria instrument BD Biosciences — Pharmingen.
B lymphoblastoid cells were used as APCs.
We hence performed cell sorting, selecting for cells positive for 2.
E11 and negative for SFR20-DQα5.
This was consistent with the IHWS HLA typing data for 9102 and verified that we had regenerated the original 9102 cell line.
The B lymphoblastoid cell lines were irradiated with 80 Gy when used in T cell assays, except the BLS transfectant, which in some experiments were irradiated with 150 Gy.
Subjects were serologically typed by a complement dependent cytotoxicity test with immunomagnetically separated target cells.
Some individuals and cell lines were genomically typed using the Olerup SSP HLA kits for DQA1 and DQB1 GenoVision, Qiagen and Dynal RELI SSO HLA kits for A, B, C and DRB1 Invitrogen.
DNA was prepared using GenoPrep Cartridge B GenoVision, Qiagen.
Gluten-specific T cells and T cell proliferation assays.
T cell reagents were established from intestinal biopsies of the celiac disease patients.
Separate, single-biopsy specimens of each subject were challenged with the following antigens: chymotrypsin-treated gluten 0.
Except for variation in the antigenic challenge of the biopsies the generation of T cell lines, T cell cloning and T cell proliferation assays were performed as described previously .
The assessment of reactivity of the T cell lines was done in proliferative restimulation assays using DR3 +DQ2 + homozygous or DR4 +DQ8 + B lymphoblastoid cells.
Positive T cell responses were defined as a stimulation index greater than 4 stimulation index calculated as mean cpm in the presence of antigen divided by mean cpm in the absence of antigen.
Activated T cells express HLA class II molecules, and to avoid autopresentation of peptides by T cells as a confounding factor in experiments with T cells of DQ2 +DQ8 + individuals, the plates with the APCs and peptides were washed thoroughly prior to the addition of T cells.
T cell clonality was tested by the IOTest Beta mark Beckman Coulter TCR Vβ staining kit covering about 70% of the normal human TCR Vβ repertoire of CD3 + lymphocytes.
For peptides 1367 and 1375, an identical amount of additional TG2 was added after 2 hours, and the incubation was continued to 4 hours.
Peptide 1378 was treated for 1.
These different incubation times were selected to obtain a similar degree of average deamidation, as determined by pilot kinetic experiments data not shown.
The reaction was stopped by adding iodoacetamide 5 mMand peptides were desalted on ZipTip columns Millipore.
Equilibration and washing steps were performed with 2% formic acid in water.
Peptides were eluted with 50% methanol, 49% water, and 1% formic acid and were analyzed for dq8 casino strats on an electrospray ionization quadrupole—time-of-flight mass spectrometer Q-Tof Ultima Global; Waters.
Samples were sprayed from needles Protana Inc.
Collision-induced dissociation was performed on the doubly charged parent ions collision gas, argon; collision energy, 25—35 electron V eV.
This work is supported by the Research Council of Norway, the European Commission, and the Deutsche Forschungsgemeinschaft.
We thank Marie Kongshaug Johannesen, Tore Jensen, and Nicole Sessler for excellent technical assistance; Anne Kari Tveter and Siri Tennebø Flåm for HLA typing; Elin Bergseng for synthesis of a peptide in the laboratory of Chaitan Khosla; Susan Radka for the kind gift of the SFR20-DQα5 hybridoma; and Erik Thorsby for critical reading of the manuscript.
MS was carried out at the Proteomic Unit, University of Bergen PROBEBergen, Norway.
Nonstandard abbreviations used: MS, mass spectrometry; P1, peptide position 1; TG2, transglutaminase 2.
Conflict of interest: The authors have declared that no conflict of interest exists.
Citation for this article: J.
Stig Tollefsen and Helene Arentz-Hansen contributed equally to this work.
Celiac disease genetics: current concepts and practical applications.
Gliadin specific, HLA DQ2-restricted T cells are commonly found in small intestinal biopsies from coeliac disease patients, but dq8 casino strats from controls.
Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells.
Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity.
Identification of a putative motif for binding of peptides to HLA-DQ2.
Allele-specific motifs characterize HLA-DQ interactions with a diabetes-associated peptide derived from glutamic acid decarboxylase.
Use of eluted peptide sequence data to identify the binding characteristics of peptides to the insulin-dependent diabetes susceptibility allele HLA-DQ8 DQ 3.
Natural peptides selected by diabetogenic DQ8 and murine I-A g7 molecules show common sequence specificity.
Identification of a gliadin T-cell epitope in coeliac disease: general importance of gliadin deamidation for intestinal T-cell recognition.
The intestinal T cell response to α-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase.
In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope.
The gluten response in children with celiac disease is directed toward multiple gliadin and glutenin peptides.
Celiac lesion T cells recognize epitopes that cluster in regions of gliadins rich in proline residues.
Refining the rules of gliadin T cell epitope binding to the disease-associated DQ2 molecule in celiac disease: importance of proline spacing and glutamine deamidation.
Small intestinal T cells of celiac disease patients recognize a natural pepsin fragment of gliadin.
Glutenin is involved in the gluten-driven mucosal T cell response.
HLA genotype distribution and genetic models of insulin-dependent diabetes mellitus.
HLA-DQβ gene contributes to susceptibility and resistance to insulin-dependent diabetes mellitus.
Invited anniversary review: HLA associated diseases.
MHC class-II molecules and autoimmunity.
Genetic control of autoimmunity in type I diabetes and associated disorders.
Genotype effects and epistasis in type 1 diabetes and HLA-DQ trans dimer associations with disease.
Structure of a human insulin peptide-HLA-DQ8 complex and susceptibility to type 1 diabetes.
nicest in michigan basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease.
MHC class II proteins and disease: a structural perspective.
Main chain hydrogen bond interactions in the binding of proline-rich gluten peptides to the Celiac disease-associated HLA-DQ2 molecule.
Structural principles of MHC class II antigen presentation.
Transcomplementation of HLA genes in IDDM.
HLA-DQ allelic polymorphisms constrain patterns of class II heterodimer formation.
Characterization of preparations of GAD65, proinsulin, and the islet tyrosine phosphatase IA-2 for use in detection of autoreactive T-cells in type 1 diabetes: report of phase II of the Second International Immunology of Diabetes Society Workshop for Standardization of T-cell assays in type 1 diabetes.
GAD65-reactive T cells are activated in patients with autoimmune type 1a diabetes.
Expanded T cells from pancreatic lymph nodes of type 1 diabetic subjects recognize an insulin epitope.
The insulin A-chain epitope recognized by human T cells is posttranslationally modified.
Production of a panel of recombinant gliadins for the characterisation of T cell reactivity in coeliac disease.
Intestinal T-cell responses to high-molecular-weight glutenins in celiac disease.
High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: implications for celiac sprue.
Characterization of an HLA-DQ2-specific monoclonal antibody.
Structural analysis of a human I-A homologue using a monoclonal antibody that recognizes an MB3-like specificity.
Human T4 + and T8 + cytotoxic T lymphocyte clones directed at products of different class II major histocompatibility complex loci.
Characterization of specific HLA-DQα allospecificities by genomic, biochemical, and serologic analysis.
HLA-DQ molecules form α-β heterodimers of mixed allotype.
Studies of gliadin-specific T cells in celiac disease.
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