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dc.contributor.author
Bergseng, Elin
dc.contributor.author
Dørum, Siri
dc.contributor.author
Arntzen, Magnus Ø.
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Nielsen, Morten
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dc.contributor.author
Nygård, Ståle
dc.contributor.author
Buus, Søren
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dc.contributor.author
de Souza, Gustavo A.
dc.contributor.author
Sollid, Ludvig M.
dc.date.available
2018-01-18T18:34:20Z
dc.date.issued
2014-12
dc.identifier.citation
Bergseng, Elin ; Dørum, Siri; Arntzen, Magnus Ø.; Nielsen, Morten; Nygård, Ståle; et al.; Different binding motifs of the celiac disease-associated HLA molecules DQ2.5, DQ2.2, and DQ7.5 revealed by relative quantitative proteomics of endogenous peptide repertoires; Springer; Immunogenetics; 67; 2; 12-2014; 73-84
dc.identifier.issn
0093-7711
dc.identifier.uri
http://hdl.handle.net/11336/33830
dc.description.abstract
Celiac disease is caused by intolerance to cereal gluten proteins, and HLA-DQ molecules are involved in the disease pathogenesis by presentation of gluten peptides to CD4+ T cells. The α- or β-chain sharing HLA molecules DQ2.5, DQ2.2, and DQ7.5 display different risks for the disease. It was recently demonstrated that T cells of DQ2.5 and DQ2.2 patients recognize distinct sets of gluten epitopes, suggesting that these two DQ2 variants select different peptides for display. To explore whether this is the case, we performed a comprehensive comparison of the endogenous self-peptides bound to HLA-DQ molecules of B-lymphoblastoid cell lines. Peptides were eluted from affinity-purified HLA molecules of nine cell lines and subjected to quadrupole orbitrap mass spectrometry and MaxQuant software analysis. Altogether, 12,712 endogenous peptides were identified at very different relative abundances. Hierarchical clustering of normalized quantitative data demonstrated significant differences in repertoires of peptides between the three DQ variant molecules. The neural network-based method, NNAlign, was used to identify peptide-binding motifs. The binding motifs of DQ2.5 and DQ7.5 concurred with previously established binding motifs. The binding motif of DQ2.2 was strikingly different from that of DQ2.5 with position P3 being a major anchor having a preference for threonine and serine. This is notable as three recently identified epitopes of gluten recognized by T cells of DQ2.2 celiac patients harbor serine at position P3. This study demonstrates that relative quantitative comparison of endogenous peptides sampled from our protein metabolism by HLA molecules provides clues to understand HLA association with disease.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Antigen Presentation/Processing
dc.subject
Celiac Disease
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Binding Motif
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Mass Spectrometry
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Mhc
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Salud Ocupacional
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dc.subject.classification
Ciencias de la Salud
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dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD
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dc.title
Different binding motifs of the celiac disease-associated HLA molecules DQ2.5, DQ2.2, and DQ7.5 revealed by relative quantitative proteomics of endogenous peptide repertoires
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-01-18T17:17:09Z
dc.identifier.eissn
1432-1211
dc.journal.volume
67
dc.journal.number
2
dc.journal.pagination
73-84
dc.journal.pais
Alemania
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dc.journal.ciudad
Berlin
dc.description.fil
Fil: Bergseng, Elin. University of Oslo; Noruega
dc.description.fil
Fil: Dørum, Siri. University of Oslo; Noruega
dc.description.fil
Fil: Arntzen, Magnus Ø.. University of Oslo; Noruega
dc.description.fil
Fil: Nielsen, Morten. Technical University of Denmark; Dinamarca. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
dc.description.fil
Fil: Nygård, Ståle. University of Oslo; Noruega
dc.description.fil
Fil: Buus, Søren. Universidad de Copenhagen; Dinamarca
dc.description.fil
Fil: de Souza, Gustavo A.. University of Oslo; Noruega
dc.description.fil
Fil: Sollid, Ludvig M.. University of Oslo; Noruega
dc.journal.title
Immunogenetics
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00251-014-0819-9
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00251-014-0819-9
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