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Cited by 16vaccines and immunoinformatics approachesImmunotherapy and Immune ResponsesCancer Immunotherapy and Biomarkers

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Mining the Immunopeptidome for Antigenic Peptides in Cancer

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León-Letelier, Ricardo A., Katayama, Hiroyuki, Hanash, Sam·2022·Cancers
DOI 10.3390/cancers14204968PMC PMC9599891
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Abstract

Although harnessing the immune system for cancer therapy has shown success, response to immunotherapy has been limited. The immunopeptidome of cancer cells presents an opportunity to discover novel antigens for immunotherapy applications. These neoantigens bind to MHC class I and class II molecules. Remarkably, the immunopeptidome encompasses protein post-translation modifications (PTMs) that may not be evident from genome or transcriptome profiling. A case in point is citrullination, which has been demonstrated to induce a strong immune response. In this review, we cover how the immunopeptidome, with a special focus on PTMs, can be utilized to identify cancer-specific antigens for immunotherapeutic applications.

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Research works printed but not linked: 119

  1. Abbott, 2019, Cancer and the Immune System: The History and Background of Immunotherapy, Semin. Oncol. Nurs., 35, 150923, 10.1016/j.soncn.2019.08.002 · DOI
  2. Kote, S., Pirog, A., Bedran, G., Alfaro, J., and Dapic, I. (2020). Mass Spectrometry-Based Identification of MHC-Associated Peptides. Cancers, 12. · DOI
  3. Okada, M., Shimizu, K., and Fujii, S.I. (2022). Identification of Neoantigens in Cancer Cells as Targets for Immunotherapy. Int. J. Mol. Sci., 23. · DOI
  4. Kotsias, 2019, Antigen processing and presentation, Int. Rev. Cell Mol. Biol., 348, 69, 10.1016/bs.ircmb.2019.07.005 · DOI · Paper page
  5. Freudenmann, 2018, Mapping the tumour human leukocyte antigen (HLA) ligandome by mass spectrometry, Immunology, 154, 331, 10.1111/imm.12936 · DOI
  6. Peters, 2017, Serine Proteases Enhance Immunogenic Antigen Presentation on Lung Cancer Cells, Cancer Immunol. Res., 5, 319, 10.1158/2326-6066.CIR-16-0141 · DOI
  7. Zhang, 2019, Application of mass spectrometry-based MHC immunopeptidome profiling in neoantigen identification for tumor immunotherapy, Biomed. Pharm., 120, 109542, 10.1016/j.biopha.2019.109542 · DOI
  8. Santambrogio, 2022, Molecular Determinants Regulating the Plasticity of the MHC Class II Immunopeptidome, Front. Immunol., 13, 878271, 10.3389/fimmu.2022.878271 · DOI
  9. Olsson, 2022, Tuning DO:DM Ratios Modulates MHC Class II Immunopeptidomes, Mol. Cell Proteom., 21, 100204, 10.1016/j.mcpro.2022.100204 · DOI
  10. Hunt, 1992, Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry, Science, 255, 1261, 10.1126/science.1546328 · DOI
  11. Yewdell, J.W. (2022). MHC Class I Immunopeptidome: Past, Present & Future. Mol. Cell Proteom., 100230. · DOI
  12. Nielsen, M., Ternette, N., and Barra, C. (2022). The interdependence of machine learning and LC-MS approaches for an unbiased understanding of the cellular immunopeptidome. Expert Rev. Proteom., 1–12. · DOI
  13. Leko, 2020, Identifying and Targeting Human Tumor Antigens for T Cell-Based Immunotherapy of Solid Tumors, Cancer Cell, 38, 454, 10.1016/j.ccell.2020.07.013 · DOI · Paper page
  14. Liepe, 2019, Mapping the MHC Class I-Spliced Immunopeptidome of Cancer Cells, Cancer Immunol. Res., 7, 62, 10.1158/2326-6066.CIR-18-0424 · DOI
  15. Mishto, 2021, Commentary: Are There Indeed Spliced Peptides in the Immunopeptidome?, Mol. Cell Proteom., 20, 100158, 10.1016/j.mcpro.2021.100158 · DOI
  16. Mishto, 2020, What We See, What We Do Not See, and What We Do Not Want to See in HLA Class I Immunopeptidomes, Proteomics, 20, e2000112, 10.1002/pmic.202000112 · DOI
  17. Katayama, H., Kobayashi, M., Irajizad, E., Sevillarno, A., Patel, N., Mao, X., Rusling, L., Vykoukal, J., Cai, Y., and Hsiao, F. (2021). Protein citrullination as a source of cancer neoantigens. J. Immunother. Cancer, 9. · DOI
  18. Wei, 2017, Varied Role of Ubiquitylation in Generating MHC Class I Peptide Ligands, J. Immunol., 198, 3835, 10.4049/jimmunol.1602122 · DOI
  19. Beresford, 2001, CIITA coordinates multiple histone acetylation modifications at the HLA-DRA promoter, Nat. Immunol., 2, 652, 10.1038/89810 · DOI
  20. McGinty, 2015, T cell epitopes and post-translationally modified epitopes in type 1 diabetes, Curr. Diab. Rep., 15, 90, 10.1007/s11892-015-0657-7 · DOI
  21. Sidney, J., Vela, J.L., Friedrich, D., Kolla, R., von Herrath, M., Wesley, J.D., and Sette, A. (2018). Low HLA binding of diabetes-associated CD8+ T-cell epitopes is increased by post translational modifications. BMC Immunol., 19. · DOI
  22. Drazic, 2016, The world of protein acetylation, Biochim. Biophys. Acta, 1864, 1372, 10.1016/j.bbapap.2016.06.007 · DOI
  23. Robert, 2011, Cancer Immunoediting: Integrating Immunity’s Roles in Cancer Suppression and Promotion, Science, 331, 1565, 10.1126/science.1203486 · DOI · Paper page
  24. Chong, 2022, Identification of tumor antigens with immunopeptidomics, Nat. Biotechnol., 40, 175, 10.1038/s41587-021-01038-8 · DOI · Paper page
  25. Sellars, 2022, Cancer vaccines: Building a bridge over troubled waters, Cell, 185, 2770, 10.1016/j.cell.2022.06.035 · DOI
  26. Gardner, 2016, Dendritic Cells and Cancer Immunity, Trends Immunol., 37, 855, 10.1016/j.it.2016.09.006 · DOI
  27. Stoitzner, P., Romani, N., Rademacher, C., Probst, H.C., and Mahnke, K. (2022). Antigen targeting to dendritic cells: Still a place in future immunotherapy?. Eur. J. Immunol., 1–16. · DOI
  28. Cook, 2018, Citrullinated alpha-enolase is an effective target for anti-cancer immunity, Oncoimmunology, 7, e1390642, 10.1080/2162402X.2017.1390642 · DOI
  29. Brentville, 2016, Citrullinated Vimentin Presented on MHC-II in Tumor Cells Is a Target for CD4+ T-Cell-Mediated Antitumor Immunity, Cancer Res., 76, 548, 10.1158/0008-5472.CAN-15-1085 · DOI · Paper page
  30. Yuzhalin, 2019, Citrullination in Cancer, Cancer Res., 79, 1274, 10.1158/0008-5472.CAN-18-2797 · DOI
  31. Turunen, 2016, Ureido group-specific antibodies are induced in rabbits immunized with citrulline or homocitrulline-containing antigens, Autoimmunity, 49, 459, 10.3109/08916934.2016.1171853 · DOI
  32. Symonds, 2021, Citrullinated Epitopes Identified on Tumour MHC Class II by Peptide Elution Stimulate Both Regulatory and Th1 Responses and Require Careful Selection for Optimal Anti-Tumour Responses, Front. Immunol., 12, 764462, 10.3389/fimmu.2021.764462 · DOI
  33. Ireland, 2011, Autophagy in antigen-presenting cells results in presentation of citrullinated peptides to CD4 T cells, J. Exp. Med., 208, 2625, 10.1084/jem.20110640 · DOI
  34. Ravanan, 2017, Autophagy: The spotlight for cellular stress responses, Life Sci., 188, 53, 10.1016/j.lfs.2017.08.029 · DOI
  35. Sase, 2017, Hypoxia-induced production of peptidylarginine deiminases and citrullinated proteins in malignant glioma cells, Biochem. Biophys. Res. Commun., 482, 50, 10.1016/j.bbrc.2016.10.154 · DOI
  36. Wang, 2021, The roles of PAD2- and PAD4-mediated protein citrullination catalysis in cancers, Int. J. Cancer, 148, 267, 10.1002/ijc.33205 · DOI
  37. Guo, 2017, Investigating the expression, effect and tumorigenic pathway of PADI2 in tumors, Onco. Targets, 10, 1475, 10.2147/OTT.S92389 · DOI
  38. Wang, 2017, PADI2-Mediated Citrullination Promotes Prostate Cancer Progression, Cancer Res., 77, 5755, 10.1158/0008-5472.CAN-17-0150 · DOI
  39. Chandrashekar, 2017, UALCAN: A Portal for Facilitating Tumor Subgroup Gene Expression and Survival Analyses, Neoplasia, 19, 649, 10.1016/j.neo.2017.05.002 · DOI · Paper page
  40. Cantarino, 2016, Downregulation of the Deiminase PADI2 Is an Early Event in Colorectal Carcinogenesis and Indicates Poor Prognosis, Mol. Cancer Res., 14, 841, 10.1158/1541-7786.MCR-16-0034 · DOI
  41. Funayama, 2017, Protein-arginine deiminase 2 suppresses proliferation of colon cancer cells through protein citrullination, Cancer Sci., 108, 713, 10.1111/cas.13179 · DOI
  42. Guertin, M.J., Zhang, X., Anguish, L., Kim, S., Varticovski, L., Lis, J.T., Hager, G.L., and Coonrod, S.A. (2014). Targeted H3R26 deimination specifically facilitates estrogen receptor binding by modifying nucleosome structure. PLoS Genet., 10. · DOI
  43. Mohanan, 2017, PAD2 overexpression in transgenic mice augments malignancy and tumor-associated inflammation in chemically initiated skin tumors, Cell Tissue Res., 370, 275, 10.1007/s00441-017-2669-x · DOI
  44. Yu, 2007, Crosstalk between cancer and immune cells: Role of STAT3 in the tumour microenvironment, Nat. Rev. Immunol., 7, 41, 10.1038/nri1995 · DOI
  45. Gijon, 2022, The Clinical and Prognostic Significance of Protein Arginine Deiminases 2 and 4 in Colorectal Cancer, Pathobiology, 89, 38, 10.1159/000518414 · DOI
  46. Xin, 2016, Role of peptidylarginine deiminase type 4 in gastric cancer, Exp. Med., 12, 3155, 10.3892/etm.2016.3798 · DOI
  47. Chang, X., Han, J., Pang, L., Zhao, Y., Yang, Y., and Shen, Z. (2009). Increased PADI4 expression in blood and tissues of patients with malignant tumors. BMC Cancer, 9. · DOI
  48. Chang, 2006, Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors, Mol. Carcinog, 45, 183, 10.1002/mc.20169 · DOI
  49. Fan, 2014, Peptidylarginine deiminase IV promotes the development of chemoresistance through inducing autophagy in hepatocellular carcinoma, Cell Biosci., 4, 49, 10.1186/2045-3701-4-49 · DOI
  50. Wang, 2010, Expression of Peptidylarginine Deiminase Type 4 in Ovarian Tumors, Int. J. Biol. Sci., 6, 454, 10.7150/ijbs.6.454 · DOI
  51. Lee, 2018, Mining the Human Tissue Proteome for Protein Citrullination, Mol. Cell Proteom., 17, 1378, 10.1074/mcp.RA118.000696 · DOI
  52. Choudhury, 2022, PAD-2-mediated citrullination of nucleophosmin provides an effective target for tumor immunotherapy, J. Immunother. Cancer, 10, e003526, 10.1136/jitc-2021-003526 · DOI
  53. Brentville, 2019, T cell repertoire to citrullinated self-peptides in healthy humans is not confined to the HLA-DR SE alleles; Targeting of citrullinated self-peptides presented by HLA-DP4 for tumour therapy, Oncoimmunology, 8, e1576490, 10.1080/2162402X.2019.1576490 · DOI
  54. Brentville, 2020, Post-translational modifications such as citrullination are excellent targets for cancer therapy, Semin. Immunol., 47, 101393, 10.1016/j.smim.2020.101393 · DOI · Paper page
  55. Singh, 2017, Phosphorylation: Implications in Cancer, Protein J., 36, 1, 10.1007/s10930-017-9696-z · DOI
  56. Song, 2019, Proteome-wide Tyrosine Phosphorylation Analysis Reveals Dysregulated Signaling Pathways in Ovarian Tumors, Mol. Cell Proteom., 18, 448, 10.1074/mcp.RA118.000851 · DOI
  57. Zarling, 2006, Identification of class I MHC-associated phosphopeptides as targets for cancer immunotherapy, Proc. Natl. Acad. Sci. USA, 103, 14889, 10.1073/pnas.0604045103 · DOI
  58. Mohammed, 2008, Phosphorylation-dependent interaction between antigenic peptides and MHC class I: A molecular basis for the presentation of transformed self, Nat. Immunol., 9, 1236, 10.1038/ni.1660 · DOI · Paper page
  59. Meyer, 2009, Identification of natural MHC class II presented phosphopeptides and tumor-derived MHC class I phospholigands, J. Proteome Res., 8, 3666, 10.1021/pr800937k · DOI
  60. Depontieu, 2009, Identification of tumor-associated, MHC class II-restricted phosphopeptides as targets for immunotherapy, Proc. Natl. Acad. Sci. USA, 106, 12073, 10.1073/pnas.0903852106 · DOI
  61. Zarling, 2014, MHC-restricted phosphopeptides from insulin receptor substrate-2 and CDC25b offer broad-based immunotherapeutic agents for cancer, Cancer Res., 74, 6784, 10.1158/0008-5472.CAN-14-0043 · DOI
  62. Cobbold, 2013, MHC Class I-Associated Phosphopeptides Are the Targets of Memory-like Immunity in Leukemia, Sci. Transl. Med., 5, 203ra125, 10.1126/scitranslmed.3006061 · DOI
  63. Tomaino, 2010, Circulating Autoantibodies to Phosphorylated a-Enolase are a Hallmark of Pancreatic Cancer, J. Proteome Res., 10, 105, 10.1021/pr100213b · DOI
  64. Mohammed, 2017, The antigenic identity of human class I MHC phosphopeptides is critically dependent upon phosphorylation status, Oncotarget, 8, 54160, 10.18632/oncotarget.16952 · DOI
  65. Alpizar, 2017, A Molecular Basis for the Presentation of Phosphorylated Peptides by HLA-B Antigens, Mol. Cell Proteom., 16, 181, 10.1074/mcp.M116.063800 · DOI
  66. Penny, 2021, Tumor Infiltrating Lymphocytes Target HLA-I Phosphopeptides Derived From Cancer Signaling in Colorectal Cancer, Front. Immunol., 12, 723566, 10.3389/fimmu.2021.723566 · DOI
  67. Stopfer, 2021, Quantitative Consequences of Protein Carriers in Immunopeptidomics and Tyrosine Phosphorylation MS(2) Analyses, Mol. Cell Proteom., 20, 100104, 10.1016/j.mcpro.2021.100104 · DOI
  68. Marcilla, 2022, Immunopeptidomic Analysis of the Phosphopeptidome Displayed by HLA Class I Molecules, Methods Mol. Biol., 2420, 149, 10.1007/978-1-0716-1936-0_12 · DOI
  69. Chen, 2019, Enrichment of Phosphorylated MHC Peptides with Immobilized Metal Affinity Chromatography and Titanium Dioxide Particles, Methods Mol. Biol., 2024, 259, 10.1007/978-1-4939-9597-4_16 · DOI
  70. Solleder, 2020, Mass Spectrometry Based Immunopeptidomics Leads to Robust Predictions of Phosphorylated HLA Class I Ligands, Mol. Cell Proteom., 19, 390, 10.1074/mcp.TIR119.001641 · DOI · Paper page
  71. Ouyang, 2022, O-GlcNAcylation and Its Role in Cancer-Associated Inflammation, Front. Immunol., 13, 861559, 10.3389/fimmu.2022.861559 · DOI
  72. Singhal, 1991, Induction of alpha-N-acetylgalactosamine-O-serine/threonine (Tn) antigen-mediated cellular immune response for active immunotherapy in mice, Cancer Res., 51, 1406
  73. Mulder, 1996, Mucin-1-related T cell infiltration in colorectal carcinoma, Cancer Immunol. Immun., 42, 351, 10.1007/s002620050293 · DOI
  74. Irazoqui, 2003, Thomsen-friedenreich disaccharide immunogenicity, Curr. Cancer Drug Targets, 3, 433, 10.2174/1568009033481714 · DOI
  75. Brockhausen, 2021, Mucins as anti-cancer targets: Perspectives of the glycobiologist, Glycoconj. J., 38, 459, 10.1007/s10719-021-09986-8 · DOI
  76. Merikhian, 2022, Recombinant nanobody against MUC1 tandem repeats inhibits growth, invasion, metastasis, and vascularization of spontaneous mouse mammary tumors, Mol. Oncol., 16, 485, 10.1002/1878-0261.13123 · DOI
  77. Laubreton, 2016, The fully synthetic MAG-Tn3 therapeutic vaccine containing the tetanus toxoid-derived TT830-844 universal epitope provides anti-tumor immunity, Cancer Immunol. Immunother., 65, 315, 10.1007/s00262-016-1802-0 · DOI
  78. 2016, Glycan Microarray Reveal the Sweet Side of Cancer Vaccines, Cell Chem. Biol., 23, 1446, 10.1016/j.chembiol.2016.12.002 · DOI
  79. Palitzsch, 2016, A Synthetic Glycopeptide Vaccine for the Induction of a Monoclonal Antibody that Differentiates between Normal and Tumor Mammary Cells and Enables the Diagnosis of Human Pancreatic Cancer, Angew. Chem. Int. Ed. Engl., 55, 2894, 10.1002/anie.201509935 · DOI
  80. Scheid, 2016, Tn-MUC1 DC Vaccination of Rhesus Macaques and a Phase I/II Trial in Patients with Nonmetastatic Castrate-Resistant Prostate Cancer, Cancer Immunol. Res., 4, 881, 10.1158/2326-6066.CIR-15-0189 · DOI · Paper page
  81. Glaffig, 2017, Immunogenicity of a Fully Synthetic MUC1 Glycopeptide Antitumor Vaccine Enhanced by Poly(I:C) as a TLR3-Activating Adjuvant, ChemMedChem, 12, 722, 10.1002/cmdc.201700254 · DOI
  82. He, Y., Schreiber, K., Wolf, S.P., Wen, F., Steentoft, C., Zerweck, J., Steiner, M., Sharma, P., Shepard, H.M., and Posey, A. (2019). Multiple cancer-specific antigens are targeted by a chimeric antigen receptor on a single cancer cell. JCI Insight., 4. · DOI
  83. Trabbic, 2021, A Stable Gold Nanoparticle-Based Vaccine for the Targeted Delivery of Tumor-Associated Glycopeptide Antigens, ACS Biol. Med. Chem. Au., 1, 31, 10.1021/acsbiomedchemau.1c00021 · DOI
  84. Trabbic, 2019, A Tumor-Selective Monoclonal Antibody from Immunization with a Tumor-Associated Mucin Glycopeptide, Sci. Rep., 9, 5662, 10.1038/s41598-019-42076-2 · DOI
  85. Zhou, 2019, CAR T Cells Targeting the Tumor MUC1 Glycoprotein Reduce Triple-Negative Breast Cancer Growth, Front. Immunol., 10, 1149, 10.3389/fimmu.2019.01149 · DOI
  86. Zhu, 2022, An efficient and safe MUC1-dendritic cell-derived exosome conjugate vaccine elicits potent cellular and humoral immunity and tumor inhibition in vivo, Acta Biomater., 138, 491, 10.1016/j.actbio.2021.10.041 · DOI
  87. Josselin, 2019, A Bispecific Antibody-Based Approach for Targeting Mesothelin in Triple Negative Breast Cancer, Front. Immunol., 10, 1593, 10.3389/fimmu.2019.01593 · DOI
  88. Qu, 2016, Molecular basis of antibody binding to mucin glycopeptides in lung cancer, Int. J. Oncol., 48, 587, 10.3892/ijo.2015.3302 · DOI
  89. Movahedin, 2017, Glycosylation of MUC1 influences the binding of a therapeutic antibody by altering the conformational equilibrium of the antigen, Glycobiology, 27, 677
  90. Marchiori, 2020, Synthesis of MUC1-derived glycopeptide bearing a novel triazole STn analog, Carbohydr. Res., 498, 108155, 10.1016/j.carres.2020.108155 · DOI
  91. Stergiou, 2021, The Development of Vaccines from Synthetic Tumor-Associated Mucin Glycopeptides and their Glycosylation-Dependent Immune Response, Chem. Rec., 21, 3313, 10.1002/tcr.202100182 · DOI
  92. Busto, 2022, Structure-based Design of Anti-cancer Vaccines: The Significance of Antigen Presentation to Boost the Immune Response, Curr. Med. Chem., 29, 1258, 10.2174/0929867328666210810152917 · DOI
  93. Doelman, W., and van Kasteren, S.I. (2022). Synthesis of glycopeptides and glycopeptide conjugates. Org. Biomol. Chem. · DOI
  94. Toraskar, 2022, The Shape of Nanostructures Encodes Immunomodulation of Carbohydrate Antigen and Vaccine Development, ACS Chem. Biol., 17, 1122, 10.1021/acschembio.1c00998 · DOI
  95. Malaker, 2017, Identification of Glycopeptides as Posttranslationally Modified Neoantigens in Leukemia, Cancer Immunol. Res., 5, 376, 10.1158/2326-6066.CIR-16-0280 · DOI
  96. Mei, 2020, Immunopeptidomic Analysis Reveals That Deamidated HLA-bound Peptides Arise Predominantly from Deglycosylated Precursors, Mol. Cell Proteom., 19, 1236, 10.1074/mcp.RA119.001846 · DOI
  97. Ferreira, 2021, Glycoproteogenomics: Setting the Course for Next-generation Cancer Neoantigen Discovery for Cancer Vaccines, Genom. Proteom. Bioinform., 19, 25, 10.1016/j.gpb.2021.03.005 · DOI
  98. Mukherjee, 2021, The HLA Ligandome Comprises a Limited Repertoire of O-GlcNAcylated Antigens Preferentially Associated With HLA-B*07:02, Front. Immunol., 12, 796584, 10.3389/fimmu.2021.796584 · DOI
  99. Pont, 2021, Site-Specific N-Linked Glycosylation Analysis of Human Carcinoembryonic Antigen by Sheathless Capillary Electrophoresis-Tandem Mass Spectrometry, J. Proteome Res., 20, 1666, 10.1021/acs.jproteome.0c00875 · DOI
  100. Hoek, 2021, Allotype-Specific Glycosylation and Cellular Localization of Human Leukocyte Antigen Class I Proteins, J. Proteome Res., 20, 4518, 10.1021/acs.jproteome.1c00466 · DOI
  101. Parker, 2021, Mapping the SARS-CoV-2 spike glycoprotein-derived peptidome presented by HLA class II on dendritic cells, Cell Rep., 35, 109179, 10.1016/j.celrep.2021.109179 · DOI
  102. Brentville, 2020, Combination vaccine based on citrullinated vimentin and enolase peptides induces potent CD4-mediated anti-tumor responses, J. Immunother. Cancer, 8, e000560, 10.1136/jitc-2020-000560 · DOI
  103. Engelhard, 2020, MHC-restricted phosphopeptide antigens: Preclinical validation and first-in-humans clinical trial in participants with high-risk melanoma, J. Immunother. Cancer, 8, e000262, 10.1136/jitc-2019-000262 · DOI
  104. Yarmarkovich, 2021, Cross-HLA targeting of intracellular oncoproteins with peptide-centric CARs, Nature, 599, 477, 10.1038/s41586-021-04061-6 · DOI
  105. Vlad, 2004, Glycoprotein tumor antigens for immunotherapy of breast cancer, Breast. Dis., 20, 73, 10.3233/BD-2004-20109 · DOI
  106. Dong, 2022, A self-adjuvanting anti-tumor nanoliposomal vaccine based on fluorine-substituted MUC1 glycopeptide, Chem. Commun., 58, 8642, 10.1039/D2CC02143A · DOI
  107. Pathangey, L.B., Lakshminarayanan, V., Suman, V.J., Pockaj, B.A., Mukherjee, P., and Gendler, S.J. (2016). Aberrant Glycosylation of Anchor-Optimized MUC1 Peptides Can Enhance Antigen Binding Affinity and Reverse Tolerance to Cytotoxic T Lymphocytes. Biomolecules, 6. · DOI
  108. Gautam, 2020, MUCIN-4 (MUC4) is a novel tumor antigen in pancreatic cancer immunotherapy, Semin. Immunol., 47, 101391, 10.1016/j.smim.2020.101391 · DOI
  109. Vigneron, 2017, Peptide splicing by the proteasome, J. Biol. Chem., 292, 21170, 10.1074/jbc.R117.807560 · DOI
  110. Feola, 2022, A novel immunopeptidomic-based pipeline for the generation of personalized oncolytic cancer vaccines, Elife, 11, e71156, 10.7554/eLife.71156 · DOI
  111. Ternette, 2018, Immunopeptidomic Profiling of HLA-A2-Positive Triple Negative Breast Cancer Identifies Potential Immunotherapy Target Antigens, Proteomics, 18, e1700465, 10.1002/pmic.201700465 · DOI
  112. Bilich, 2020, Mass spectrometry-based identification of a B-cell maturation antigen-derived T-cell epitope for antigen-specific immunotherapy of multiple myeloma, Blood Cancer J., 10, 24, 10.1038/s41408-020-0288-3 · DOI
  113. Marcu, 2021, HLA Ligand Atlas: A benign reference of HLA-presented peptides to improve T-cell-based cancer immunotherapy, J. Immunother. Cancer, 9, e002071, 10.1136/jitc-2020-002071 · DOI · Paper page
  114. Heard, 2022, Antigen glycosylation regulates efficacy of CAR T cells targeting CD19, Nat. Commun., 13, 3367, 10.1038/s41467-022-31035-7 · DOI
  115. Raglow, 2022, Targeting Glycans for CAR Therapy: The Advent of Sweet CARs, Mol. Ther., 30, 2881, 10.1016/j.ymthe.2022.07.006 · DOI
  116. Irving, 2022, A roadmap for driving CAR T cells toward the oncogenic immunopeptidome, Cancer Cell, 40, 20, 10.1016/j.ccell.2021.12.011 · DOI
  117. Bonifaz, 2019, OMIC signatures to understand cancer immunosurveillance and immunoediting: Melanoma and immune cells interplay in immunotherapy, J. Leukoc. Biol., 105, 915, 10.1002/JLB.MR0618-241RR · DOI
  118. Mantilla, 2020, Induction of Progenitor Exhausted Tissue-Resident Memory CD8(+) T Cells Upon Salmonella Typhi Porins Adjuvant Immunization Correlates With Melanoma Control and Anti-PD-1 Immunotherapy Cooperation, Front. Immunol., 11, 583382, 10.3389/fimmu.2020.583382 · DOI
  119. Ott, 2017, An immunogenic personal neoantigen vaccine for patients with melanoma, Nature, 547, 217, 10.1038/nature22991 · DOI · Paper page

Metadata

Authors
León-Letelier, R. A., Katayama, H., & Hanash, S.
Affiliations
  • Clinical Cancer Prevention, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA
  • The University of Texas MD Anderson Cancer Center (US)
ORCID
Venue
Cancers
Publisher
MDPI AG
Published
2022-10-11
Volume
14
Issue
20
Pages
4968
ISSN
2072-6694 (ISSN-L)
DOI
10.3390/cancers14204968
PMC
PMC9599891
OpenAlex
W4304185593
Cited by
16
References
1
Citations by year
2026: 2 · 2025: 2 · 2024: 5 · 2023: 7
FWCI
0.36
Type
journal article
Language
en
Open access
Licence
Locations
  • Cancers (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
  • Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
  • Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
Keywords
immunopeptidome, neoantigens, antigenic peptides, cancer immunotherapy, MHC class I, MHC class II, post-translational modification, citrullination, tumor-specific antigens

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Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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