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Journal articles on the topic 'Immunopeptome'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Kuznetsov, Alexandr, Alice Voronina, Vadim Govorun, and Georgij Arapidi. "Critical Review of Existing MHC I Immunopeptidome Isolation Methods." Molecules 25, no. 22 (2020): 5409. http://dx.doi.org/10.3390/molecules25225409.

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Major histocompatibility complex class I (MHC I) plays a crucial role in the development of adaptive immune response in vertebrates. MHC molecules are cell surface protein complexes loaded with short peptides and recognized by the T-cell receptors (TCR). Peptides associated with MHC are named immunopeptidome. The MHC I immunopeptidome is produced by the proteasome degradation of intracellular proteins. The knowledge of the immunopeptidome repertoire facilitates the creation of personalized antitumor or antiviral vaccines. A huge number of publications on the immunopeptidome diversity of differ

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2

Peltonen, Karita, Sara Feola, Husen M. Umer, et al. "Therapeutic Cancer Vaccination with Immunopeptidomics-Discovered Antigens Confers Protective Antitumor Efficacy." Cancers 13, no. 14 (2021): 3408. http://dx.doi.org/10.3390/cancers13143408.

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Knowledge of clinically targetable tumor antigens is becoming vital for broader design and utility of therapeutic cancer vaccines. This information is obtained reliably by directly interrogating the MHC-I presented peptide ligands, the immunopeptidome, with state-of-the-art mass spectrometry. Our manuscript describes direct identification of novel tumor antigens for an aggressive triple-negative breast cancer model. Immunopeptidome profiling revealed 2481 unique antigens, among them a novel ERV antigen originating from an endogenous retrovirus element. The clinical benefit and tumor control po

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3

Spangelo, Bryan L., and Robert M. Macleod. "Immunopeptide Regulation of Anterior Pituitary Function." International Journal of Neuroscience 51, no. 3-4 (1990): 369–70. http://dx.doi.org/10.3109/00207459008999747.

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4

Georgiadou, Dimitra, and Efstratios Stratikos. "Cellular Mechanisms that Edit the Immunopeptidome." Current Proteomics 6, no. 1 (2009): 13–24. http://dx.doi.org/10.2174/157016409787847439.

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5

Perreault, Claude, Pierre Thibault, and Guido Kroemer. "A bacterium-derived, cancer-associated immunopeptidome." OncoImmunology 10, no. 1 (2021): 1918373. http://dx.doi.org/10.1080/2162402x.2021.1918373.

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6

Walz, Juliane Sarah. "The immunopeptidome guides permissive HLA mismatch." Blood 137, no. 7 (2021): 864–65. http://dx.doi.org/10.1182/blood.2020009266.

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7

Yewdell, Jonathan W., and Michael F. Princiotta. "All roads lead to “ome”: defining the DRiPome." Blood 119, no. 26 (2012): 6179–80. http://dx.doi.org/10.1182/blood-2012-04-420810.

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In this issue of Blood, Granados et al explore the relationship between the cellular transcriptome and immunopeptidome,1,2 the repertoire of peptides presented by MHC class I molecules for immunosurveillance.

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8

Dudek, N. L., C. T. Tan, D. G. Gorasia, N. P. Croft, P. T. Illing, and A. W. Purcell. "Constitutive and Inflammatory Immunopeptidome of Pancreatic -Cells." Diabetes 61, no. 11 (2012): 3018–25. http://dx.doi.org/10.2337/db11-1333.

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9

Bräunlein, Eva, and Angela M. Krackhardt. "Tools to define the melanoma-associated immunopeptidome." Immunology 152, no. 4 (2017): 536–44. http://dx.doi.org/10.1111/imm.12803.

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10

Erhard, Florian, Lars Dölken, Bastian Schilling, and Andreas Schlosser. "Identification of the Cryptic HLA-I Immunopeptidome." Cancer Immunology Research 8, no. 8 (2020): 1018–26. http://dx.doi.org/10.1158/2326-6066.cir-19-0886.

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11

Perreault, Claude, Diana Granados, Céline Laumont, and Pierre Thibault. "The immunopeptidome of normal and neoplastic cells." Experimental Hematology 42, no. 8 (2014): S5. http://dx.doi.org/10.1016/j.exphem.2014.07.017.

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12

Hartholt, Robin B., Ivan Peyron, and Jan Voorberg. "Hunting down factor VIII in the immunopeptidome." Cellular Immunology 301 (March 2016): 59–64. http://dx.doi.org/10.1016/j.cellimm.2015.11.001.

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13

Admon, Arie. "ERAP1 shapes just part of the immunopeptidome." Human Immunology 80, no. 5 (2019): 296–301. http://dx.doi.org/10.1016/j.humimm.2019.03.004.

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14

Admon, Arie. "Are There Indeed Spliced Peptides in the Immunopeptidome?" Molecular & Cellular Proteomics 20 (2021): 100099. http://dx.doi.org/10.1016/j.mcpro.2021.100099.

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15

Faridi, Pouya, Chen Li, Sri H. Ramarathinam, et al. "A subset of HLA-I peptides are not genomically templated: Evidence for cis- and trans-spliced peptide ligands." Science Immunology 3, no. 28 (2018): eaar3947. http://dx.doi.org/10.1126/sciimmunol.aar3947.

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The diversity of peptides displayed by class I human leukocyte antigen (HLA) plays an essential role in T cell immunity. The peptide repertoire is extended by various posttranslational modifications, including proteasomal splicing of peptide fragments from distinct regions of an antigen to form nongenomically templated cis-spliced sequences. Previously, it has been suggested that a fraction of the immunopeptidome constitutes such cis-spliced peptides; however, because of computational limitations, it has not been possible to assess whether trans-spliced peptides (i.e., the fusion of peptide se

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16

Zhang, Lichao, Patrick L. McAlpine, Marlene L. Heberling, and Joshua E. Elias. "Automated Ligand Purification Platform Accelerates Immunopeptidome Analysis by Mass Spectrometry." Journal of Proteome Research 20, no. 1 (2020): 393–408. http://dx.doi.org/10.1021/acs.jproteome.0c00464.

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17

Pfammatter, Sibylle, Eric Bonneil, Joel Lanoix, et al. "Extending the Comprehensiveness of Immunopeptidome Analyses Using Isobaric Peptide Labeling." Analytical Chemistry 92, no. 13 (2020): 9194–204. http://dx.doi.org/10.1021/acs.analchem.0c01545.

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18

Narayan, Rupa, Niclas Olsson, Lisa E. Wagar, et al. "Acute myeloid leukemia immunopeptidome reveals HLA presentation of mutated nucleophosmin." PLOS ONE 14, no. 7 (2019): e0219547. http://dx.doi.org/10.1371/journal.pone.0219547.

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19

Fortier, Marie-Hélène, Etienne Caron, Danielle De Verteuil, Claude Perreault, and Pierre Thibault. "Influence of mTOR Signalling Pathway on the MHC I Immunopeptidome." Blood 110, no. 11 (2007): 3887. http://dx.doi.org/10.1182/blood.v110.11.3887.3887.

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Abstract Cell surface major histocompatibility complex (MHC) I molecules are associated with self peptides that are collectively referred to as the self MHC I immunopeptidome (sMII). Despite the tremendous importance of the sMII, very little is known on its genesis and molecular composition. On the other hand, it is well established that the signalling pathway involving mammalian target of rapamycin (mTOR) plays an essential role in the regulation of processes such as ribosome biogenesis and protein translation which are critical for cell growth, proliferation and differentiation. In this work

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20

Gravett, A. M., S. Stevanović, A. G. Dalgleish, and J. Copier. "Gemcitabine alters the proteasome composition and immunopeptidome of tumour cells." OncoImmunology 7, no. 6 (2018): e1438107. http://dx.doi.org/10.1080/2162402x.2018.1438107.

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21

Synowsky, Silvia A., Sally L. Shirran, Fiona G. M. Cooke, Antony N. Antoniou, Catherine H. Botting, and Simon J. Powis. "The major histocompatibility complex class I immunopeptidome of extracellular vesicles." Journal of Biological Chemistry 292, no. 41 (2017): 17084–92. http://dx.doi.org/10.1074/jbc.m117.805895.

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22

Sofron, Adriana, Danilo Ritz, Dario Neri, and Tim Fugmann. "High-resolution analysis of the murine MHC class II immunopeptidome." European Journal of Immunology 46, no. 2 (2015): 319–28. http://dx.doi.org/10.1002/eji.201545930.

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23

Liepe, Juliane, John Sidney, Felix K. M. Lorenz, Alessandro Sette, and Michele Mishto. "Mapping the MHC Class I–Spliced Immunopeptidome of Cancer Cells." Cancer Immunology Research 7, no. 1 (2018): 62–76. http://dx.doi.org/10.1158/2326-6066.cir-18-0424.

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24

Ruiz Cuevas, Maria Virginia, Marie-Pierre Hardy, Jaroslav Hollý, et al. "Most non-canonical proteins uniquely populate the proteome or immunopeptidome." Cell Reports 34, no. 10 (2021): 108815. http://dx.doi.org/10.1016/j.celrep.2021.108815.

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25

Joyce, Peter, Lesley Young, Martin Quibell, et al. "446 Immunopeptidome changes mediated by a novel ERAP1 inhibitor leads to tumor growth inhibition." Journal for ImmunoTherapy of Cancer 8, Suppl 3 (2020): A472. http://dx.doi.org/10.1136/jitc-2020-sitc2020.0446.

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BackgroundClinical data demonstrates increased antigen presentation diversity is a key factor in determining response rates to checkpoint inhibitors.1 In addition to tumour mutational burden/microsatellite instability, increased HLA heterozygosity and HLA evolutionary diversity are non-overlapping factors recently identified to further diversify the immunopeptidome and improve clinical response to checkpoint therapies.2 3 Endoplasmic reticulum aminopeptidase 1 (ERAP1) is an enzyme that trims peptides loaded into classical and nonclassical class I MHC molecules.4 5 Ablation of mouse ERAAP modif

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26

Roerden, Malte, Annika Nelde, Jonas S. Heitmann, et al. "HLA Evolutionary Divergence as a Prognostic Marker for AML Patients Undergoing Allogeneic Stem Cell Transplantation." Cancers 12, no. 7 (2020): 1835. http://dx.doi.org/10.3390/cancers12071835.

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The diversity of human leukocyte antigens (HLAs) enables the presentation of immense repertoires of peptides, including tumor-associated antigens (TAAs). As a surrogate for immunopeptidome diversity, the HLA evolutionary divergence (HED) between individual HLA alleles might directly define the ability to present TAAs, a prerequisite for graft-versus-leukemia effects. We therefore analyzed the impact of HED on survival within a cohort of 171 acute myeloid leukemia (AML) patients after matched donor allogeneic hematopoietic stem cell transplantation (HSCT). Low HED (<25th percentile) of HLA c

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27

van Balen, Peter, Michel G. D. Kester, Wendy de Klerk, et al. "Immunopeptidome Analysis of HLA-DPB1 Allelic Variants Reveals New Functional Hierarchies." Journal of Immunology 204, no. 12 (2020): 3273–82. http://dx.doi.org/10.4049/jimmunol.2000192.

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28

Zaitouna, Anita J., Amanpreet Kaur, and Malini Raghavan. "Variations in MHC class I antigen presentation and immunopeptidome selection pathways." F1000Research 9 (September 28, 2020): 1177. http://dx.doi.org/10.12688/f1000research.26935.1.

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Major histocompatibility class I (MHC-I) proteins mediate immunosurveillance against pathogens and cancers by presenting antigenic or mutated peptides to antigen receptors of CD8+ T cells and by engaging receptors of natural killer (NK) cells. In humans, MHC-I molecules are highly polymorphic. MHC-I variations permit the display of thousands of distinct peptides at the cell surface. Recent mass spectrometric studies have revealed unique and shared characteristics of the peptidomes of individual MHC-I variants. The cell surface expression of MHC-I–peptide complexes requires the functions of man

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29

Hickman, H. D., and J. W. Yewdell. "Mining the plasma immunopeptidome for cancer peptides as biomarkers and beyond." Proceedings of the National Academy of Sciences 107, no. 44 (2010): 18747–48. http://dx.doi.org/10.1073/pnas.1013851107.

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30

Faridi, Pouya, Katherine Woods, Simone Ostrouska, et al. "Spliced Peptides and Cytokine-Driven Changes in the Immunopeptidome of Melanoma." Cancer Immunology Research 8, no. 10 (2020): 1322–34. http://dx.doi.org/10.1158/2326-6066.cir-19-0894.

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31

Tedeschi, Valentina, Giorgia Paldino, Fabiana Paladini, et al. "The Impact of the ‘Mis-Peptidome’ on HLA Class I-Mediated Diseases: Contribution of ERAP1 and ERAP2 and Effects on the Immune Response." International Journal of Molecular Sciences 21, no. 24 (2020): 9608. http://dx.doi.org/10.3390/ijms21249608.

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The strong association with the Major Histocompatibility Complex (MHC) class I genes represents a shared trait for a group of autoimmune/autoinflammatory disorders having in common immunopathogenetic basis as well as clinical features. Accordingly, the main risk factors for Ankylosing Spondylitis (AS), prototype of the Spondyloarthropathies (SpA), the Behçet’s disease (BD), the Psoriasis (Ps) and the Birdshot Chorioretinopathy (BSCR) are HLA-B*27, HLA-B*51, HLA-C*06:02 and HLA-A*29:02, respectively. Despite the strength of the association, the HLA pathogenetic role in these diseases is far fro

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32

Vizcaíno, Juan Antonio, Peter Kubiniok, Kevin A. Kovalchik, et al. "The Human Immunopeptidome Project: A Roadmap to Predict and Treat Immune Diseases." Molecular & Cellular Proteomics 19, no. 1 (2019): 31–49. http://dx.doi.org/10.1074/mcp.r119.001743.

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33

Knudson, C. M., J. R. Mickelson, C. F. Louis, and K. P. Campbell. "Distinct immunopeptide maps of the sarcoplasmic reticulum Ca2+ release channel in malignant hyperthermia." Journal of Biological Chemistry 265, no. 5 (1990): 2421–24. http://dx.doi.org/10.1016/s0021-9258(19)39813-8.

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34

Admon, Arie, and Michal Bassani-Sternberg. "The Human Immunopeptidome Project, a Suggestion for yet another Postgenome Next Big Thing." Molecular & Cellular Proteomics 10, no. 10 (2011): O111.011833. http://dx.doi.org/10.1074/mcp.o111.011833.

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35

Colbert, Jeff D., and Kenneth L. Rock. "How a tailor achieves the perfect fit." Journal of Biological Chemistry 295, no. 21 (2020): 7211–12. http://dx.doi.org/10.1074/jbc.h120.013868.

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Most antigenic peptides that bind stably to a major histocompatibility complex (MHC) I molecule for display to the immune system are approximately the same length, thanks in part to the expert trimming done by endoplasmic reticulum aminopeptidases (ERAPs), the final peptidases in the antigen-presentation pathway. An open question is whether ERAPs edit peptides to this optimal length while they are bound to MHC I molecules (using the latter as a pattern of sorts) or by free hand. Mavridis et al. present multiple lines of evidence that this trimming cannot readily occur on MHC I molecules, but r

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36

Brown, Scott D., and Robert A. Holt. "Neoantigen characteristics in the context of the complete predicted MHC class I self-immunopeptidome." OncoImmunology 8, no. 3 (2018): 1556080. http://dx.doi.org/10.1080/2162402x.2018.1556080.

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37

Knierman, Michael D., Megan B. Lannan, Laura J. Spindler, Carl L. McMillian, Robert J. Konrad, and Robert W. Siegel. "The Human Leukocyte Antigen Class II Immunopeptidome of the SARS-CoV-2 Spike Glycoprotein." Cell Reports 33, no. 9 (2020): 108454. http://dx.doi.org/10.1016/j.celrep.2020.108454.

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38

Faridi, Pouya, Ruedi Aebersold, and Etienne Caron. "A first dataset toward a standardized community-driven global mapping of the human immunopeptidome." Data in Brief 7 (June 2016): 201–5. http://dx.doi.org/10.1016/j.dib.2016.02.016.

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39

Zhang, Xiaomei, Yue Qi, Qi Zhang, and Wei Liu. "Application of mass spectrometry-based MHC immunopeptidome profiling in neoantigen identification for tumor immunotherapy." Biomedicine & Pharmacotherapy 120 (December 2019): 109542. http://dx.doi.org/10.1016/j.biopha.2019.109542.

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40

van Hateren, Andy, and Tim Elliott. "The role of MHC I protein dynamics in tapasin and TAPBPR-assisted immunopeptidome editing." Current Opinion in Immunology 70 (June 2021): 138–43. http://dx.doi.org/10.1016/j.coi.2021.06.016.

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41

Mohan, Sonali V., Keshava K. Datta, Rebekah Ziegman, Corey Smith, and Harsha Gowda. "Protocol for purification and identification of MHC class I immunopeptidome from cancer cell lines." STAR Protocols 2, no. 1 (2021): 100385. http://dx.doi.org/10.1016/j.xpro.2021.100385.

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42

Bilich, Tatjana, Simon D. Walz, Annika Nelde, et al. "Analysis of the Multiple Myeloma HLA Peptidome Identifies a Naturally Presented Bcma-Derived Peptide As an Immunogenic T-Cell Epitope for Immunotherapeutic Approaches." Blood 132, Supplement 1 (2018): 3173. http://dx.doi.org/10.1182/blood-2018-99-113473.

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Abstract The B-cell maturation antigen (BCMA) is selectively expressed by cells of the B-lineage, including multiple myeloma (MM) cells, and constitutes a promising target for immunotherapeutic approaches. At present, BCMA is being evaluated as target for immunotherapeutic approaches, such as CAR T cells and bispecific antibodies, which have demonstrated promising results in phase I clinical trials. The utilization of cytotoxic T cells bearing T-cell receptors against BCMA constitutes an alternative promising approach to target MM cells. Therefore, the identification of BCMA-derived peptides t

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43

Fugmann, Tim, Adriana Sofron, Danilo Ritz, Franziska Bootz, and Dario Neri. "The MHC Class II Immunopeptidome of Lymph Nodes in Health and in Chemically Induced Colitis." Journal of Immunology 198, no. 3 (2016): 1357–64. http://dx.doi.org/10.4049/jimmunol.1601157.

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44

Rajaraman, Srinath, Denis Canjuga, Michael Ghosh, et al. "Measles Virus-Based Treatments Trigger a Pro-inflammatory Cascade and a Distinctive Immunopeptidome in Glioblastoma." Molecular Therapy - Oncolytics 12 (March 2019): 147–61. http://dx.doi.org/10.1016/j.omto.2018.12.010.

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45

Altmann, Daniel M. "New tools for MHC research from machine learning and predictive algorithms to the tumour immunopeptidome." Immunology 154, no. 3 (2018): 329–30. http://dx.doi.org/10.1111/imm.12956.

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46

Fortier, Marie-Hélène, Etienne Caron, Marie-Pierre Hardy, et al. "The MHC I Immunopeptidome Is Moulded by the Transcriptome and Conceals a Tissue-Specific Signature." Blood 110, no. 11 (2007): 1327. http://dx.doi.org/10.1182/blood.v110.11.1327.1327.

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Abstract Background: Cell surface MHC I molecules are associated with self peptides that are collectively referred to as the self MHC I immunopeptidome (sMII). The sMII plays vital roles: it shapes the repertoire of developing thymocytes, transmits survival signals to mature CD8 T cells, amplifies responses against intracellular pathogens, allows immunosurveillance of neoplastic cells, and influences mating preferences in mice. Despite the tremendous importance of the sMII, very little is known on its genesis and molecular composition. Methodology/Principal Findings: We developed a novel high-

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47

Lanoix, Joël, Chantal Durette, Mathieu Courcelles, et al. "Comparison of the MHC I Immunopeptidome Repertoire of B-Cell Lymphoblasts Using Two Isolation Methods." PROTEOMICS 18, no. 12 (2018): 1700251. http://dx.doi.org/10.1002/pmic.201700251.

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48

Caron, Etienne, Krystel Vincent, Marie‐Hélène Fortier, et al. "The MHC I immunopeptidome conveys to the cell surface an integrative view of cellular regulation." Molecular Systems Biology 7, no. 1 (2011): 533. http://dx.doi.org/10.1038/msb.2011.68.

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49

Mangalaparthi, Kiran K., Anil K. Madugundu, Zachary C. Ryan, et al. "Digging deeper into the immunopeptidome: characterization of post-translationally modified peptides presented by MHC I." Journal of Proteins and Proteomics 12, no. 3 (2021): 151–60. http://dx.doi.org/10.1007/s42485-021-00066-x.

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50

Scull, Katherine E., Nadine L. Dudek, Alexandra J. Corbett, et al. "Secreted HLA recapitulates the immunopeptidome and allows in-depth coverage of HLA A*02:01 ligands." Molecular Immunology 51, no. 2 (2012): 136–42. http://dx.doi.org/10.1016/j.molimm.2012.02.117.

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