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Exploration of peptides bound to MHC class I molecules in melanoma.

Identifieur interne : 001801 ( Main/Merge ); précédent : 001800; suivant : 001802

Exploration of peptides bound to MHC class I molecules in melanoma.

Auteurs : Antonia L. Pritchard [Australie] ; Marcus L. Hastie ; Michelle Neller ; Jeffrey J. Gorman ; Chris W. Schmidt ; Nicholas K. Hayward

Source :

RBID : pubmed:25645385

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English descriptors

Abstract

Advancements in high-resolution HPLC and mass spectrometry have reinvigorated the application of this technology to identify peptides eluted from immunopurified MHC class I molecules. Three melanoma cell lines were assessed using w6/32 isolation, peptide elution and HPLC purification; peptides were identified by mass spectrometry. A total of 13,829 peptides were identified; 83-87% of these were 8-11 mers. Only approximately 15% have been described before. Subcellular locations of the source proteins showed even sampling; mRNA expression and total protein length were predictive of the number of peptides detected from a single protein. HLA-type binding prediction for 10,078 9/10 mer peptides assigned 88-95% to a patient-specific HLA subtype, revealing a disparity in strength of predicted binding. HLA-B*27-specific isolation successfully identified some peptides not found using w6/32. Sixty peptides were selected for immune screening, based on source protein and predicted HLA binding; no new peptides recognized by antimelanoma T cells were discovered. Additionally, mass spectrometry was unable to identify several epitopes targeted ex vivo by one patient's T cells.

DOI: 10.1111/pcmr.12357
PubMed: 25645385

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pubmed:25645385

Le document en format XML

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<title level="j">Pigment cell & melanoma research</title>
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<term>Algorithms</term>
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<term>Antigens, Neoplasm (metabolism)</term>
<term>Cell Line, Tumor</term>
<term>Epitopes</term>
<term>Gene Expression Regulation, Neoplastic</term>
<term>Histocompatibility Antigens Class I (metabolism)</term>
<term>Humans</term>
<term>Immunity</term>
<term>Mass Spectrometry</term>
<term>Melanoma (genetics)</term>
<term>Melanoma (immunology)</term>
<term>Molecular Sequence Data</term>
<term>Peptides (chemistry)</term>
<term>Peptides (isolation & purification)</term>
<term>Peptides (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Processing, Post-Translational</term>
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<term>Antigènes d'histocompatibilité de classe I (métabolisme)</term>
<term>Antigènes néoplasiques (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Fractions subcellulaires (métabolisme)</term>
<term>Humains</term>
<term>Immunité</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire tumorale</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Mélanome (génétique)</term>
<term>Mélanome (immunologie)</term>
<term>Peptides ()</term>
<term>Peptides (isolement et purification)</term>
<term>Peptides (métabolisme)</term>
<term>Reproductibilité des résultats</term>
<term>Régulation de l'expression des gènes tumoraux</term>
<term>Spectrométrie de masse</term>
<term>Séquence d'acides aminés</term>
<term>Épitopes</term>
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<term>Peptides</term>
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<term>Antigens, Neoplasm</term>
<term>Histocompatibility Antigens Class I</term>
<term>Peptides</term>
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<term>Melanoma</term>
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<term>Melanoma</term>
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<term>Peptides</term>
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<term>Immunity</term>
<term>Mass Spectrometry</term>
<term>Molecular Sequence Data</term>
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<term>Protein Processing, Post-Translational</term>
<term>Reproducibility of Results</term>
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<term>Données de séquences moléculaires</term>
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<term>Immunité</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire tumorale</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Peptides</term>
<term>Reproductibilité des résultats</term>
<term>Régulation de l'expression des gènes tumoraux</term>
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<front>
<div type="abstract" xml:lang="en">Advancements in high-resolution HPLC and mass spectrometry have reinvigorated the application of this technology to identify peptides eluted from immunopurified MHC class I molecules. Three melanoma cell lines were assessed using w6/32 isolation, peptide elution and HPLC purification; peptides were identified by mass spectrometry. A total of 13,829 peptides were identified; 83-87% of these were 8-11 mers. Only approximately 15% have been described before. Subcellular locations of the source proteins showed even sampling; mRNA expression and total protein length were predictive of the number of peptides detected from a single protein. HLA-type binding prediction for 10,078 9/10 mer peptides assigned 88-95% to a patient-specific HLA subtype, revealing a disparity in strength of predicted binding. HLA-B*27-specific isolation successfully identified some peptides not found using w6/32. Sixty peptides were selected for immune screening, based on source protein and predicted HLA binding; no new peptides recognized by antimelanoma T cells were discovered. Additionally, mass spectrometry was unable to identify several epitopes targeted ex vivo by one patient's T cells.</div>
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