- Main chain hydrogen bond interactions in the binding of proline-rich gluten peptides to the celiac disease-associated HLA-DQ2 moleculeElin Bergseng
Institute of Immunology, University of Oslo, Rikshospitalet University Hospital, N 0027 Oslo, Norway
J Biol Chem 280:21791-6. 2005..This is a unique feature of DQ2 and is likely a key parameter for preferential binding of proline-rich gluten peptides and development of celiac disease...
- Differences in the risk of celiac disease associated with HLA-DQ2.5 or HLA-DQ2.2 are related to sustained gluten antigen presentationLars Egil Fallang
Centre for Immune Regulation, Institute of Immunology, University of Oslo and Oslo University Hospital Rikshospitalet, Oslo, Norway
Nat Immunol 10:1096-101. 2009..2 (phenylalanine) cannot. Our findings suggest that the kinetic stability of complexes of peptide and major histocompatibility complex (MHC) is of importance for the association of HLA with disease...
- Refining the rules of gliadin T cell epitope binding to the disease-associated DQ2 molecule in celiac disease: importance of proline spacing and glutamine deamidationShuo Wang Qiao
Institute of Immunology, University of Oslo, Rikshospitalet University Hospital, Oslo, Norway
J Immunol 175:254-61. 2005..Contrary to previous findings, our data do not show selective presentation of DQ2.5 over DQ2.2 for gluten epitopes that carry proline residues at the P3 position...
- Analysis of the binding of gluten T-cell epitopes to various human leukocyte antigen class II moleculesElin Bergseng
Centre for Immune Regulation and Institute of Immunology, Rikshospitalet University Hospital, N 0027 Oslo, Norway
Hum Immunol 69:94-100. 2008..The results demonstrate that the gluten T-cell epitopes mainly bind to the DQ2 molecule...
- Antigen presentation to celiac lesion-derived T cells of a 33-mer gliadin peptide naturally formed by gastrointestinal digestionShuo Wang Qiao
Institute of Immunology, Rikshospitalet University Hospital, University of Oslo, Oslo, Norway
J Immunol 173:1757-62. 2004..The 33-mer is thus a potent T cell stimulator that does not require further processing within APC for T cell presentation and that binds to DQ2 with a pH profile that promotes extracellular binding...
- Complexes of two cohorts of CLIP peptides and HLA-DQ2 of the autoimmune DR3-DQ2 haplotype are poor substrates for HLA-DMLars Egil Fallang
Centre for Immune Regulation and Institute of Immunology, University of Oslo, Oslo, Norway
J Immunol 181:5451-61. 2008..We suggest that the unusual interaction of DQ2 with Ii and DM may provide a basis for the known disease associations of DQ2...
- Soluble HLA-DQ2 expressed in S2 cells copurifies with a high affinity insect cell derived proteinUlrike Jüse
Centre for Immune Regulation, Institute of Immunology, University of Oslo, Oslo, Norway
Immunogenetics 61:81-9. 2009..Further mapping of this fragment of 54 residues identified a pentadecapeptide with high affinity for sDQ2 which may serve as a lead compound for the design of HLA-DQ2 blockers...
- Tetramer visualization of gut-homing gluten-specific T cells in the peripheral blood of celiac disease patientsMelinda Raki
Institute of Immunology, University of Oslo, Rikshospitalet Radiumhospitalet Medical Center, 0027 Oslo, Norway
Proc Natl Acad Sci U S A 104:2831-6. 2007..Most of the cells had a memory phenotype, but many other phenotypic markers showed a heterogeneous pattern. Tetramer staining of gluten-specific T cells has the potential to be used for diagnosis of celiac disease...
- Cyclic and dimeric gluten peptide analogues inhibiting DQ2-mediated antigen presentation in celiac diseaseJiang Xia
Department of Chemistry, Stanford University, Stanford, CA 94305 5025, USA
Bioorg Med Chem 15:6565-73. 2007..One dimeric peptide analogue with an intermediate linker length was found to be especially effective at inhibiting DQ2 mediated antigen presentation. The implications of these findings for the treatment of celiac disease are discussed...
- Inhibition of HLA-DQ2-mediated antigen presentation by analogues of a high affinity 33-residue peptide from alpha2-gliadinJiang Xia
Departments of Chemistry, Chemical Engineering, and Biochemistry, Stanford University, Stanford, CA 94305 5025, USA
J Am Chem Soc 128:1859-67. 2006....
- Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac diseaseChu Young Kim
Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA
Proc Natl Acad Sci U S A 101:4175-9. 2004..Finally, surface-exposed proline residues in the proteolytically resistant ligand were replaced with functionalized analogs, thereby providing a starting point for the design of orally active agents for blocking gluten-induced toxicity...