메뉴 건너뛰기




Volumn 46, Issue 2, 2017, Pages 315-326

Mass Spectrometry Profiling of HLA-Associated Peptidomes in Mono-allelic Cells Enables More Accurate Epitope Prediction

(15)  Abelin, Jennifer G a   Keskin, Derin B a,b,c,d,h   Sarkizova, Siranush a,b   Hartigan, Christina R a   Zhang, Wandi c   Sidney, John e   Stevens, Jonathan d   Lane, William d   Zhang, Guang Lan b,c,h   Eisenhaure, Thomas M a   Clauser, Karl R a   Hacohen, Nir a,c,i   Rooney, Michael S a,f,g   Carr, Steven A a   Wu, Catherine J a,b,c,d  


Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; PROTEASOME; HLA ANTIGEN CLASS 1; PEPTIDE;

EID: 85013878753     PISSN: 10747613     EISSN: 10974180     Source Type: Journal    
DOI: 10.1016/j.immuni.2017.02.007     Document Type: Article
Times cited : (456)

References (58)
  • 1
    • 84959881509 scopus 로고    scopus 로고
    • Gapped sequence alignment using artificial neural networks: application to the MHC class I system
    • Andreatta, M., Nielsen, M., Gapped sequence alignment using artificial neural networks: application to the MHC class I system. Bioinformatics 32 (2016), 511–517.
    • (2016) Bioinformatics , vol.32 , pp. 511-517
    • Andreatta, M.1    Nielsen, M.2
  • 2
    • 84988940043 scopus 로고    scopus 로고
    • Unsupervised HLA peptidome deconvolution improves ligand prediction accuracy and predicts cooperative effects in peptide-HLA interactions
    • Bassani-Sternberg, M., Gfeller, D., Unsupervised HLA peptidome deconvolution improves ligand prediction accuracy and predicts cooperative effects in peptide-HLA interactions. J. Immunol. 197 (2016), 2492–2499.
    • (2016) J. Immunol. , vol.197 , pp. 2492-2499
    • Bassani-Sternberg, M.1    Gfeller, D.2
  • 3
    • 84924326106 scopus 로고    scopus 로고
    • Mass spectrometry of human leukocyte antigen class I peptidomes reveals strong effects of protein abundance and turnover on antigen presentation
    • Bassani-Sternberg, M., Pletscher-Frankild, S., Jensen, L.J., Mann, M., Mass spectrometry of human leukocyte antigen class I peptidomes reveals strong effects of protein abundance and turnover on antigen presentation. Mol. Cell. Proteomics 14 (2015), 658–673.
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 658-673
    • Bassani-Sternberg, M.1    Pletscher-Frankild, S.2    Jensen, L.J.3    Mann, M.4
  • 4
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends, C., Sowa, M.E., Gygi, S.P., Harper, J.W., Network organization of the human autophagy system. Nature 466 (2010), 68–76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 5
    • 33646743956 scopus 로고    scopus 로고
    • Detection of artifacts and peptide modifications in liquid chromatography/mass spectrometry data using two-dimensional signal intensity map data visualization
    • Berg, M., Parbel, A., Pettersen, H., Fenyö, D., Björkesten, L., Detection of artifacts and peptide modifications in liquid chromatography/mass spectrometry data using two-dimensional signal intensity map data visualization. Rapid Commun. Mass Spectrom. 20 (2006), 1558–1562.
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 1558-1562
    • Berg, M.1    Parbel, A.2    Pettersen, H.3    Fenyö, D.4    Björkesten, L.5
  • 6
    • 84899080404 scopus 로고    scopus 로고
    • The nature and extent of contributions by defective ribosome products to the HLA peptidome
    • Bourdetsky, D., Schmelzer, C.E.H., Admon, A., The nature and extent of contributions by defective ribosome products to the HLA peptidome. Proc. Natl. Acad. Sci. USA 111 (2014), E1591–E1599.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E1591-E1599
    • Bourdetsky, D.1    Schmelzer, C.E.H.2    Admon, A.3
  • 7
    • 77958576252 scopus 로고    scopus 로고
    • An integrated approach to epitope analysis I: Dimensional reduction, visualization and prediction of MHC binding using amino acid principal components and regression approaches
    • Bremel, R.D., Homan, E.J., An integrated approach to epitope analysis I: Dimensional reduction, visualization and prediction of MHC binding using amino acid principal components and regression approaches. Immunome Res., 6, 2010, 7.
    • (2010) Immunome Res. , vol.6 , pp. 7
    • Bremel, R.D.1    Homan, E.J.2
  • 12
    • 84904256267 scopus 로고    scopus 로고
    • ERAP1-ERAP2 dimerization increases peptide-trimming efficiency
    • Evnouchidou, I., Weimershaus, M., Saveanu, L., van Endert, P., ERAP1-ERAP2 dimerization increases peptide-trimming efficiency. J. Immunol. 193 (2014), 901–908.
    • (2014) J. Immunol. , vol.193 , pp. 901-908
    • Evnouchidou, I.1    Weimershaus, M.2    Saveanu, L.3    van Endert, P.4
  • 13
    • 80053074684 scopus 로고    scopus 로고
    • CONSeQuence: prediction of reference peptides for absolute quantitative proteomics using consensus machine learning approaches
    • Eyers, C.E., Lawless, C., Wedge, D.C., Lau, K.W., Gaskell, S.J., Hubbard, S.J., CONSeQuence: prediction of reference peptides for absolute quantitative proteomics using consensus machine learning approaches. Mol. Cell. Proteomics, 10, 2011, 003384.
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. 003384
    • Eyers, C.E.1    Lawless, C.2    Wedge, D.C.3    Lau, K.W.4    Gaskell, S.J.5    Hubbard, S.J.6
  • 14
    • 59849093889 scopus 로고    scopus 로고
    • Prediction of high-responding peptides for targeted protein assays by mass spectrometry
    • Fusaro, V.A., Mani, D.R., Mesirov, J.P., Carr, S.A., Prediction of high-responding peptides for targeted protein assays by mass spectrometry. Nat. Biotechnol. 27 (2009), 190–198.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 190-198
    • Fusaro, V.A.1    Mani, D.R.2    Mesirov, J.P.3    Carr, S.A.4
  • 15
    • 0025612425 scopus 로고
    • Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence
    • Guruprasad, K., Reddy, B.V.B., Pandit, M.W., Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Eng. 4 (1990), 155–161.
    • (1990) Protein Eng. , vol.4 , pp. 155-161
    • Guruprasad, K.1    Reddy, B.V.B.2    Pandit, M.W.3
  • 20
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y., Oda, Y., Tabata, T., Sato, T., Nagasu, T., Rappsilber, J., Mann, M., Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol. Cell. Proteomics 4 (2005), 1265–1272.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 21
    • 84889637320 scopus 로고    scopus 로고
    • NetMHCstab—Predicting stability of peptide-MHC-I complexes; impacts for cytotoxic T lymphocyte epitope discovery
    • Jørgensen, K.W., Rasmussen, M., Buus, S., Nielsen, M., NetMHCstab—Predicting stability of peptide-MHC-I complexes; impacts for cytotoxic T lymphocyte epitope discovery. Immunology 141 (2014), 18–26.
    • (2014) Immunology , vol.141 , pp. 18-26
    • Jørgensen, K.W.1    Rasmussen, M.2    Buus, S.3    Nielsen, M.4
  • 22
    • 70449338115 scopus 로고    scopus 로고
    • Systematic characterisation of cellular localisation and expression profiles of proteins containing MHC ligands
    • Juncker, A.S., Larsen, M.V., Weinhold, N., Nielsen, M., Brunak, S., Lund, O., Systematic characterisation of cellular localisation and expression profiles of proteins containing MHC ligands. PLoS ONE, 4, 2009, e7448.
    • (2009) PLoS ONE , vol.4 , pp. e7448
    • Juncker, A.S.1    Larsen, M.V.2    Weinhold, N.3    Nielsen, M.4    Brunak, S.5    Lund, O.6
  • 24
    • 71949096416 scopus 로고    scopus 로고
    • Derivation of an amino acid similarity matrix for peptide: MHC binding and its application as a Bayesian prior
    • Kim, Y., Sidney, J., Pinilla, C., Sette, A., Peters, B., Derivation of an amino acid similarity matrix for peptide: MHC binding and its application as a Bayesian prior. BMC Bioinformatics, 10, 2009, 394.
    • (2009) BMC Bioinformatics , vol.10 , pp. 394
    • Kim, Y.1    Sidney, J.2    Pinilla, C.3    Sette, A.4    Peters, B.5
  • 25
    • 84873489169 scopus 로고    scopus 로고
    • Positional bias of MHC class I restricted T-cell epitopes in viral antigens is likely due to a bias in conservation
    • Kim, Y., Yewdell, J.W., Sette, A., Peters, B., Positional bias of MHC class I restricted T-cell epitopes in viral antigens is likely due to a bias in conservation. PLoS Comput. Biol., 9, 2013, e1002884.
    • (2013) PLoS Comput. Biol. , vol.9 , pp. e1002884
    • Kim, Y.1    Yewdell, J.W.2    Sette, A.3    Peters, B.4
  • 28
    • 84859210032 scopus 로고    scopus 로고
    • Fast gapped-read alignment with Bowtie 2
    • Langmead, B., Salzberg, S.L., Fast gapped-read alignment with Bowtie 2. Nat. Methods 9 (2012), 357–359.
    • (2012) Nat. Methods , vol.9 , pp. 357-359
    • Langmead, B.1    Salzberg, S.L.2
  • 29
    • 79961123152 scopus 로고    scopus 로고
    • RSEM: Accurate transcript quantification from RNA-Seq data with or without a reference genome
    • Li, B., Dewey, C.N., RSEM: Accurate transcript quantification from RNA-Seq data with or without a reference genome. BMC Bioinformatics, 12, 2011, 323.
    • (2011) BMC Bioinformatics , vol.12 , pp. 323
    • Li, B.1    Dewey, C.N.2
  • 32
    • 48449106045 scopus 로고    scopus 로고
    • NetMHC-3.0: accurate web accessible predictions of human, mouse and monkey MHC class I affinities for peptides of length 8-11
    • W509-12
    • Lundegaard, C., Lamberth, K., Harndahl, M., Buus, S., Lund, O., Nielsen, M., NetMHC-3.0: accurate web accessible predictions of human, mouse and monkey MHC class I affinities for peptides of length 8-11. Nucleic Acids Res., 36, 2008 W509-12.
    • (2008) Nucleic Acids Res. , vol.36
    • Lundegaard, C.1    Lamberth, K.2    Harndahl, M.3    Buus, S.4    Lund, O.5    Nielsen, M.6
  • 34
    • 33644701579 scopus 로고    scopus 로고
    • The turnover kinetics of major histocompatibility complex peptides of human cancer cells
    • Milner, E., Barnea, E., Beer, I., Admon, A., The turnover kinetics of major histocompatibility complex peptides of human cancer cells. Mol. Cell. Proteomics 5 (2006), 357–365.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 357-365
    • Milner, E.1    Barnea, E.2    Beer, I.3    Admon, A.4
  • 36
    • 84921925151 scopus 로고    scopus 로고
    • Abundance-based classifier for the prediction of mass spectrometric peptide detectability upon enrichment (PPA)
    • Muntel, J., Boswell, S.A., Tang, S., Ahmed, S., Wapinski, I., Foley, G., Steen, H., Springer, M., Abundance-based classifier for the prediction of mass spectrometric peptide detectability upon enrichment (PPA). Mol. Cell. Proteomics 14 (2015), 430–440.
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 430-440
    • Muntel, J.1    Boswell, S.A.2    Tang, S.3    Ahmed, S.4    Wapinski, I.5    Foley, G.6    Steen, H.7    Springer, M.8
  • 37
    • 17844385106 scopus 로고    scopus 로고
    • The role of the proteasome in generating cytotoxic T-cell epitopes: Insights obtained from improved predictions of proteasomal cleavage
    • Nielsen, M., Lundegaard, C., Lund, O., Keşmir, C., The role of the proteasome in generating cytotoxic T-cell epitopes: Insights obtained from improved predictions of proteasomal cleavage. Immunogenetics 57 (2005), 33–41.
    • (2005) Immunogenetics , vol.57 , pp. 33-41
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Keşmir, C.4
  • 39
    • 85013913295 scopus 로고    scopus 로고
    • Peptides: Calculate indices and theoretical physicochemical properties of peptides and protein sequences.
    • D. Osorio, P. Rondón-Villarreal, R. Torres (2014). Peptides: Calculate indices and theoretical physicochemical properties of peptides and protein sequences. http://CRAN.R-project.org/package=Peptides. R Package Version 1.1.0.
    • (2014)
    • Osorio, D.1    Rondón-Villarreal, P.2    Torres, R.3
  • 41
    • 33748335464 scopus 로고    scopus 로고
    • Elicitation from virus-naive individuals of cytotoxic T lymphocytes directed against conserved HIV-1 epitopes
    • Reche, P.A., Keskin, D.B., Hussey, R.E., Ancuta, P., Gabuzda, D., Reinherz, E.L., Elicitation from virus-naive individuals of cytotoxic T lymphocytes directed against conserved HIV-1 epitopes. Med. Immunol., 5, 2006, 1.
    • (2006) Med. Immunol. , vol.5 , pp. 1
    • Reche, P.A.1    Keskin, D.B.2    Hussey, R.E.3    Ancuta, P.4    Gabuzda, D.5    Reinherz, E.L.6
  • 45
    • 0038350948 scopus 로고    scopus 로고
    • Predicting proteasomal cleavage sites: A comparison of available methods
    • Saxová, P., Buus, S., Brunak, S., Keşmir, C., Predicting proteasomal cleavage sites: A comparison of available methods. Int. Immunol. 15 (2003), 781–787.
    • (2003) Int. Immunol. , vol.15 , pp. 781-787
    • Saxová, P.1    Buus, S.2    Brunak, S.3    Keşmir, C.4
  • 46
    • 84928770388 scopus 로고    scopus 로고
    • Neoantigens in cancer immunotherapy
    • Schumacher, T.N., Schreiber, R.D., Neoantigens in cancer immunotherapy. Science 348 (2015), 69–74.
    • (2015) Science , vol.348 , pp. 69-74
    • Schumacher, T.N.1    Schreiber, R.D.2
  • 47
    • 84940547175 scopus 로고    scopus 로고
    • Using data independent acquisition (DIA) to model high-responding peptides for targeted proteomics experiments
    • Searle, B.C., Egertson, J.D., Bollinger, J.G., Stergachis, A.B., MacCoss, M.J., Using data independent acquisition (DIA) to model high-responding peptides for targeted proteomics experiments. Mol. Cell. Proteomics 14 (2015), 2331–2340.
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 2331-2340
    • Searle, B.C.1    Egertson, J.D.2    Bollinger, J.G.3    Stergachis, A.B.4    MacCoss, M.J.5
  • 49
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M.E., Bennett, E.J., Gygi, S.P., Harper, J.W., Defining the human deubiquitinating enzyme interaction landscape. Cell 138 (2009), 389–403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 50
    • 85042682207 scopus 로고    scopus 로고
    • Theano: A Python framework for fast computation of mathematical expressions
    • Theano Development Team. Theano: A Python framework for fast computation of mathematical expressions. ArXiv, 2016 https://arxiv.org/abs/1605.02688.
    • (2016) ArXiv
  • 53
    • 84958568837 scopus 로고    scopus 로고
    • The length distribution of class I–restricted T cell epitopes is determined by both peptide supply and MHC allele-specific binding preference
    • Trolle, T., McMurtrey, C.P., Sidney, J., Bardet, W., Osborn, S.C., Kaever, T., Sette, A., Hildebrand, W.H., Nielsen, M., Peters, B., The length distribution of class I–restricted T cell epitopes is determined by both peptide supply and MHC allele-specific binding preference. J. Immunol. 196 (2016), 1480–1487.
    • (2016) J. Immunol. , vol.196 , pp. 1480-1487
    • Trolle, T.1    McMurtrey, C.P.2    Sidney, J.3    Bardet, W.4    Osborn, S.C.5    Kaever, T.6    Sette, A.7    Hildebrand, W.H.8    Nielsen, M.9    Peters, B.10
  • 54
    • 84861151032 scopus 로고    scopus 로고
    • Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition
    • Udeshi, N.D., Mani, D.R., Eisenhaure, T., Mertins, P., Jaffe, J.D., Clauser, K.R., Hacohen, N., Carr, S.A., Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Mol. Cell. Proteomics 11 (2012), 148–159.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 148-159
    • Udeshi, N.D.1    Mani, D.R.2    Eisenhaure, T.3    Mertins, P.4    Jaffe, J.D.5    Clauser, K.R.6    Hacohen, N.7    Carr, S.A.8
  • 55
    • 84874619400 scopus 로고    scopus 로고
    • Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments
    • Udeshi, N.D., Svinkina, T., Mertins, P., Kuhn, E., Mani, D.R., Qiao, J.W., Carr, S.A., Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Mol. Cell. Proteomics 12 (2013), 825–831.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 825-831
    • Udeshi, N.D.1    Svinkina, T.2    Mertins, P.3    Kuhn, E.4    Mani, D.R.5    Qiao, J.W.6    Carr, S.A.7
  • 57
    • 82455192402 scopus 로고    scopus 로고
    • DRiPs solidify: Progress in understanding endogenous MHC class I antigen processing
    • Yewdell, J.W., DRiPs solidify: Progress in understanding endogenous MHC class I antigen processing. Trends Immunol. 32 (2011), 548–558.
    • (2011) Trends Immunol. , vol.32 , pp. 548-558
    • Yewdell, J.W.1
  • 58
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • York, I.A., Chang, S.-C., Saric, T., Keys, J.A., Favreau, J.M., Goldberg, A.L., Rock, K.L., The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat. Immunol. 3 (2002), 1177–1184.
    • (2002) Nat. Immunol. , vol.3 , pp. 1177-1184
    • York, I.A.1    Chang, S.-C.2    Saric, T.3    Keys, J.A.4    Favreau, J.M.5    Goldberg, A.L.6    Rock, K.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.