Exploration of peptides bound to MHC class I molecules in melanoma.
Identifieur interne : 001711 ( PubMed/Corpus ); précédent : 001710; suivant : 001712Exploration of peptides bound to MHC class I molecules in melanoma.
Auteurs : Antonia L. Pritchard ; Marcus L. Hastie ; Michelle Neller ; Jeffrey J. Gorman ; Chris W. Schmidt ; Nicholas K. HaywardSource :
- Pigment cell & melanoma research [ 1755-148X ] ; 2015.
English descriptors
- KwdEn :
- Algorithms, Amino Acid Sequence, Antibodies (metabolism), Antigens, Neoplasm (metabolism), Cell Line, Tumor, Epitopes, Gene Expression Regulation, Neoplastic, Histocompatibility Antigens Class I (metabolism), Humans, Immunity, Mass Spectrometry, Melanoma (genetics), Melanoma (immunology), Molecular Sequence Data, Peptides (chemistry), Peptides (isolation & purification), Peptides (metabolism), Protein Binding, Protein Processing, Post-Translational, RNA, Messenger (genetics), RNA, Messenger (metabolism), Reproducibility of Results, Subcellular Fractions (metabolism).
- MESH :
- chemical , chemistry : Peptides.
- chemical , genetics : RNA, Messenger.
- chemical , isolation & purification : Peptides.
- chemical , metabolism : Antibodies, Antigens, Neoplasm, Histocompatibility Antigens Class I, Peptides, RNA, Messenger.
- genetics : Melanoma.
- immunology : Melanoma.
- metabolism : Subcellular Fractions.
- Algorithms, Amino Acid Sequence, Cell Line, Tumor, Epitopes, Gene Expression Regulation, Neoplastic, Humans, Immunity, Mass Spectrometry, Molecular Sequence Data, Protein Binding, Protein Processing, Post-Translational, Reproducibility of Results.
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
Links to Exploration step
pubmed:25645385Le document en format XML
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<author><name sortKey="Pritchard, Antonia L" sort="Pritchard, Antonia L" uniqKey="Pritchard A" first="Antonia L" last="Pritchard">Antonia L. Pritchard</name>
<affiliation><nlm:affiliation>Oncogenomics Research Group, QIMR Berghofer Medical Research Institute, Herston, Brisbane, Qld, Australia.</nlm:affiliation>
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<author><name sortKey="Hastie, Marcus L" sort="Hastie, Marcus L" uniqKey="Hastie M" first="Marcus L" last="Hastie">Marcus L. Hastie</name>
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<author><name sortKey="Neller, Michelle" sort="Neller, Michelle" uniqKey="Neller M" first="Michelle" last="Neller">Michelle Neller</name>
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<author><name sortKey="Gorman, Jeffrey J" sort="Gorman, Jeffrey J" uniqKey="Gorman J" first="Jeffrey J" last="Gorman">Jeffrey J. Gorman</name>
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<author><name sortKey="Schmidt, Chris W" sort="Schmidt, Chris W" uniqKey="Schmidt C" first="Chris W" last="Schmidt">Chris W. Schmidt</name>
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<author><name sortKey="Hayward, Nicholas K" sort="Hayward, Nicholas K" uniqKey="Hayward N" first="Nicholas K" last="Hayward">Nicholas K. Hayward</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Exploration of peptides bound to MHC class I molecules in melanoma.</title>
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<series><title level="j">Pigment cell & melanoma research</title>
<idno type="eISSN">1755-148X</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algorithms</term>
<term>Amino Acid Sequence</term>
<term>Antibodies (metabolism)</term>
<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>
<term>RNA, Messenger (genetics)</term>
<term>RNA, Messenger (metabolism)</term>
<term>Reproducibility of Results</term>
<term>Subcellular Fractions (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptides</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>RNA, Messenger</term>
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<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Peptides</term>
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<term>Antigens, Neoplasm</term>
<term>Histocompatibility Antigens Class I</term>
<term>Peptides</term>
<term>RNA, Messenger</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Melanoma</term>
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<term>Amino Acid Sequence</term>
<term>Cell Line, Tumor</term>
<term>Epitopes</term>
<term>Gene Expression Regulation, Neoplastic</term>
<term>Humans</term>
<term>Immunity</term>
<term>Mass Spectrometry</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Processing, Post-Translational</term>
<term>Reproducibility of Results</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>
</front>
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<ArticleTitle>Exploration of peptides bound to MHC class I molecules in melanoma.</ArticleTitle>
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<Abstract><AbstractText>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.</AbstractText>
<CopyrightInformation>© 2015 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.</CopyrightInformation>
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<ForeName>Antonia L</ForeName>
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