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Article ; Online: Arid5a: A Missing Link between EMT and Tumoral Immune Resistance.

Van den Eynde, Benoit J

2021 Volume 9, Issue 8, Page(s) 854

Abstract: Epithelial-to-mesenchymal transition (EMT) endows tumor cells with the ability to invade and migrate, and to suppress antitumor immunity. In this issue, Parajuli and colleagues report that EMT tumors often express the RNA-binding protein AT-rich ... ...

Abstract	Epithelial-to-mesenchymal transition (EMT) endows tumor cells with the ability to invade and migrate, and to suppress antitumor immunity. In this issue, Parajuli and colleagues report that EMT tumors often express the RNA-binding protein AT-rich interactive domain 5a (Arid5a), which they find stabilizes the mRNAs encoding indoleamine 2,3 dioxygenase (IDO1) and CCL2. As a new link between EMT and tumoral immune resistance, Arid5a represents a therapeutic target of interest.
MeSH term(s)	Animals ; DNA-Binding Proteins ; Mice ; Mice, Inbred C57BL ; RNA, Messenger ; RNA-Binding Proteins ; Transcription Factors/metabolism
Chemical Substances	Arid5a protein, mouse ; DNA-Binding Proteins ; RNA, Messenger ; RNA-Binding Proteins ; Transcription Factors
Language	English
Publishing date	2021-06-22
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2732489-8
ISSN	2326-6074 ; 2326-6066
ISSN (online)	2326-6074
ISSN	2326-6066
DOI	10.1158/2326-6066.CIR-21-0432
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Article ; Online: Editorial: Heme proteins: key players in the regulation of immune responses.

Volpi, Claudia / Van den Eynde, Benoît J / Orabona, Ciriana

Frontiers in immunology

2023 Volume 14, Page(s) 1263384

MeSH term(s)	Hemeproteins ; Immunity
Chemical Substances	Hemeproteins
Language	English
Publishing date	2023-08-09
Publishing country	Switzerland
Document type	Editorial ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1263384
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Article ; Online: Combining personalized neoantigen vaccination with chemotherapy and anti-PD-1 to treat NSCLC.

Leung, Carol Sze Ki / Van den Eynde, Benoit J

Cancer cell

2022 Volume 40, Issue 9, Page(s) 903–905

Abstract: In this issue of Cancer Cell, Awad et al. report a phase 1b clinical trial combining a personalized vaccine NEO-PV-01 with chemotherapy and anti-PD-1 pembrolizumab in first-line metastatic non-squamous NSCLC. They demonstrate that this treatment regimen ... ...

Abstract	In this issue of Cancer Cell, Awad et al. report a phase 1b clinical trial combining a personalized vaccine NEO-PV-01 with chemotherapy and anti-PD-1 pembrolizumab in first-line metastatic non-squamous NSCLC. They demonstrate that this treatment regimen was well tolerated and induced neoantigen-specific CD4
MeSH term(s)	Antineoplastic Combined Chemotherapy Protocols/therapeutic use ; Carcinoma, Non-Small-Cell Lung/drug therapy ; Carcinoma, Non-Small-Cell Lung/pathology ; Clinical Trials, Phase I as Topic ; Humans ; Lung Neoplasms/pathology ; Vaccination
Language	English
Publishing date	2022-08-25
Publishing country	United States
Document type	Introductory Journal Article ; Comment
ZDB-ID	2078448-X
ISSN	1878-3686 ; 1535-6108
ISSN (online)	1878-3686
ISSN	1535-6108
DOI	10.1016/j.ccell.2022.08.002
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Zs.A 5650: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 104: Show issues

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Article ; Online: Functional Differences between Proteasome Subtypes.

Abi Habib, Joanna / Lesenfants, Julie / Vigneron, Nathalie / Van den Eynde, Benoit J

Cells

2022 Volume 11, Issue 3

Abstract: Four proteasome subtypes are commonly present in mammalian tissues: standard proteasomes, which contain the standard catalytic subunits β1, β2 and β5; immunoproteasomes containing the immuno-subunits β1i, β2i and β5i; and two intermediate proteasomes, ... ...

Abstract	Four proteasome subtypes are commonly present in mammalian tissues: standard proteasomes, which contain the standard catalytic subunits β1, β2 and β5; immunoproteasomes containing the immuno-subunits β1i, β2i and β5i; and two intermediate proteasomes, containing a mix of standard and immuno-subunits. Recent studies revealed the expression of two tissue-specific proteasome subtypes in cortical thymic epithelial cells and in testes: thymoproteasomes and spermatoproteasomes. In this review, we describe the mechanisms that enable the ATP- and ubiquitin-dependent as well as the ATP- and ubiquitin-independent degradation of proteins by the proteasome. We focus on understanding the role of the different proteasome subtypes in maintaining protein homeostasis in normal physiological conditions through the ATP- and ubiquitin-dependent degradation of proteins. Additionally, we discuss the role of each proteasome subtype in the ATP- and ubiquitin-independent degradation of disordered proteins. We also discuss the role of the proteasome in the generation of peptides presented by MHC class I molecules and the implication of having different proteasome subtypes for the peptide repertoire presented at the cell surface. Finally, we discuss the role of the immunoproteasome in immune cells and its modulation as a potential therapy for autoimmune diseases.
MeSH term(s)	Adenosine Triphosphate ; Animals ; Cytoplasm/metabolism ; Histocompatibility Antigens Class I ; Mammals/metabolism ; Peptides ; Proteasome Endopeptidase Complex/metabolism ; Ubiquitin
Chemical Substances	Histocompatibility Antigens Class I ; Peptides ; Ubiquitin ; Adenosine Triphosphate (8L70Q75FXE) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2022-01-26
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11030421
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Article: Systemic tryptophan homeostasis.

Klaessens, Simon / Stroobant, Vincent / De Plaen, Etienne / Van den Eynde, Benoit J

Frontiers in molecular biosciences

2022 Volume 9, Page(s) 897929

Abstract: Tryptophan is an essential amino acid, which is not only a building block for protein synthesis, but also a precursor for the biosynthesis of co-enzymes and neuromodulators, such as NAD/NADP(H), kynurenic acid, melatonin and serotonin. It also plays a ... ...

Abstract	Tryptophan is an essential amino acid, which is not only a building block for protein synthesis, but also a precursor for the biosynthesis of co-enzymes and neuromodulators, such as NAD/NADP(H), kynurenic acid, melatonin and serotonin. It also plays a role in immune homeostasis, as local tryptophan catabolism impairs T-lymphocyte mediated immunity. Therefore, tryptophan plasmatic concentration needs to be stable, in spite of large variations in dietary supply. Here, we review the main checkpoints accounting for tryptophan homeostasis, including absorption, transport, metabolism and elimination, and we discuss the physiopathology of disorders associated with their dysfunction. Tryptophan is catabolized along the kynurenine pathway through the action of two enzymes that mediate the first and rate-limiting step of the pathway: indoleamine 2,3-dioxygenase 1 (IDO1) and tryptophan 2,3-dioxygenase (TDO). While IDO1 expression is restricted to peripheral sites of immune modulation, TDO is massively expressed in the liver and accounts for 90% of tryptophan catabolism. Recent data indicated that the stability of the TDO protein is regulated by tryptophan and that this regulation allows a tight control of tryptophanemia. TDO is stabilized when tryptophan is abundant in the plasma, resulting in rapid degradation of dietary tryptophan. In contrast, when tryptophan is scarce, TDO is degraded by the proteasome to avoid excessive tryptophan catabolism. This is triggered by the unmasking of a degron in a non-catalytic tryptophan-binding site, resulting in TDO ubiquitination by E3 ligase SKP1-CUL1-F-box. Deficiency in TDO or in the hepatic aromatic transporter SLC16A10 leads to severe hypertryptophanemia, which can disturb immune and neurological homeostasis.
Language	English
Publishing date	2022-09-14
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2022.897929
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Article ; Online: Metformin improves cancer immunotherapy by directly rescuing tumor-infiltrating CD8 T lymphocytes from hypoxia-induced immunosuppression.

Finisguerra, Veronica / Dvorakova, Tereza / Formenti, Matteo / Van Meerbeeck, Pierre / Mignion, Lionel / Gallez, Bernard / Van den Eynde, Benoit J

Journal for immunotherapy of cancer

2023 Volume 11, Issue 5

Abstract: Background: Despite their revolutionary success in cancer treatment over the last decades, immunotherapies encounter limitations in certain tumor types and patients. The efficacy of immunotherapies depends on tumor antigen-specific CD8 T-cell viability ... ...

Abstract	Background: Despite their revolutionary success in cancer treatment over the last decades, immunotherapies encounter limitations in certain tumor types and patients. The efficacy of immunotherapies depends on tumor antigen-specific CD8 T-cell viability and functionality within the immunosuppressive tumor microenvironment, where oxygen levels are often low. Hypoxia can reduce CD8 T-cell fitness in several ways and CD8 T cells are mostly excluded from hypoxic tumor regions. Given the challenges to achieve durable reduction of hypoxia in the clinic, ameliorating CD8 T-cell survival and effector function in hypoxic condition could improve tumor response to immunotherapies. Methods: Activated CD8 T cells were exposed to hypoxia and metformin and analyzed by fluorescence-activated cell sorting for cell proliferation, apoptosis and phenotype. In vivo, metformin was administered to mice bearing hypoxic tumors and receiving either adoptive cell therapy with tumor-specific CD8 T cells, or immune checkpoint inhibitors; tumor growth was followed over time and CD8 T-cell infiltration, survival and localization in normoxic or hypoxic tumor regions were assessed by flow cytometry and immunofluorescence. Tumor oxygenation and hypoxia were measured by electron paramagnetic resonance and pimonidazole staining, respectively. Results: We found that the antidiabetic drug metformin directly improved CD8 T-cell fitness in hypoxia, both in vitro and in vivo. Metformin rescued murine and human CD8 T cells from hypoxia-induced apoptosis and increased their proliferation and cytokine production, while blunting the upregulation of programmed cell death protein 1 and lymphocyte-activation gene 3. This appeared to result from a reduced production of reactive oxygen species, due to the inhibition of mitochondrial complex I. Differently from what others reported, metformin did not reduce tumor hypoxia, but rather increased CD8 T-cell infiltration and survival in hypoxic tumor areas, and synergized with cyclophosphamide to enhance tumor response to adoptive cell therapy or immune checkpoint blockade in different tumor models. Conclusions: This study describes a novel mechanism of action of metformin and presents a promising strategy to achieve immune rejection in hypoxic and immunosuppressive tumors, which would otherwise be resistant to immunotherapy.
MeSH term(s)	Humans ; Animals ; Mice ; Metformin/pharmacology ; Metformin/therapeutic use ; Neoplasms/drug therapy ; Neoplasms/pathology ; CD8-Positive T-Lymphocytes ; Immunotherapy ; Immunosuppression Therapy ; Immunosuppressive Agents ; Hypoxia ; Tumor Microenvironment
Chemical Substances	Metformin (9100L32L2N) ; Immunosuppressive Agents
Language	English
Publishing date	2023-05-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2719863-7
ISSN	2051-1426 ; 2051-1426
ISSN (online)	2051-1426
ISSN	2051-1426
DOI	10.1136/jitc-2022-005719
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Article ; Online: Tumour immune rejection triggered by activation of α2-adrenergic receptors.

Zhu, Jingjing / Naulaerts, Stefan / Boudhan, Loubna / Martin, Manon / Gatto, Laurent / Van den Eynde, Benoit J

Nature

2023 Volume 618, Issue 7965, Page(s) 607–615

Abstract: Immunotherapy based on immunecheckpoint blockade (ICB) using antibodies induces rejection of tumours and brings clinical benefit in patients with various cancer ... ...

Abstract	Immunotherapy based on immunecheckpoint blockade (ICB) using antibodies induces rejection of tumours and brings clinical benefit in patients with various cancer types
MeSH term(s)	Animals ; Humans ; Mice ; CD4-Positive T-Lymphocytes/drug effects ; CD4-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/drug effects ; CD8-Positive T-Lymphocytes/immunology ; Neoplasms/drug therapy ; Neoplasms/immunology ; Signal Transduction/drug effects ; Tumor Microenvironment ; Receptors, Adrenergic, alpha-2/metabolism ; Adrenergic alpha-2 Receptor Agonists/pharmacology ; Adrenergic alpha-2 Receptor Agonists/therapeutic use ; Adrenergic alpha-2 Receptor Antagonists/pharmacology ; Macrophages/drug effects ; Macrophages/immunology ; Mice, Knockout ; Single-Cell Gene Expression Analysis
Chemical Substances	Receptors, Adrenergic, alpha-2 ; Adrenergic alpha-2 Receptor Agonists ; Adrenergic alpha-2 Receptor Antagonists ; Adra2a protein, mouse ; ADRA2A protein, human
Language	English
Publishing date	2023-06-07
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-023-06110-8
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: TGFβ1 neutralization displays therapeutic efficacy through both an immunomodulatory and a non-immune tumor-intrinsic mechanism.

Canè, Stefania / Van Snick, Jacques / Uyttenhove, Catherine / Pilotte, Luc / Van den Eynde, Benoit J

Journal for immunotherapy of cancer

2021 Volume 9, Issue 2

Abstract: Background: Transforming growth factor-β (TGFβ) is emerging as a promising target for cancer therapy, given its ability to promote progression of advanced tumors and to suppress anti-tumor immune responses. However, TGFβ also plays multiple roles in ... ...

Abstract	Background: Transforming growth factor-β (TGFβ) is emerging as a promising target for cancer therapy, given its ability to promote progression of advanced tumors and to suppress anti-tumor immune responses. However, TGFβ also plays multiple roles in normal tissues, particularly during organogenesis, raising toxicity concerns about TGFβ blockade. Dose-limiting cardiovascular toxicity was observed, possibly due to the blockade of all three TGFβ isoforms. The dominant isoform in tumors is TGFβ1, while TGFβ2 and TGFβ3 seem to be more involved in cardiovascular development. Recent data indicated that selective targeting of TGFβ1 promoted the efficacy of checkpoint inhibitor anti-PD1 in transplanted preclinical tumor models, without cardiovascular toxicity. Methods: To further explore the therapeutic potential of isoform-specific TGFβ blockade, we developed neutralizing mAbs targeting mature TGFβ1 or TGFβ3, and tested them, in parallel with anti-panTGFβ mAb 1D11, in two preclinical models: the transplanted colon cancer model CT26, and the autochthonous melanoma model TiRP. Results: We observed that the blockade of TGFβ1, but not that of TGFβ3, increased the efficacy of a prophylactic cellular vaccine against colon cancer CT26. This effect was similar to pan-TGFβ blockade, and was associated with increased infiltration of activated CD8 T cells in the tumor, and reduced levels of regulatory T cells and myeloid-derived suppressor cells. In contrast, in the autochthonous TiRP melanoma model, we observed therapeutic efficacy of the TGFβ1-specific mAb as a single agent, while the TGFβ3 mAb was inactive. In this model, the anti-tumor effect of TGFβ1 blockade was tumor intrinsic rather than immune mediated, as it was also observed in T-cell depleted mice. Mechanistically, TGFβ1 blockade increased mouse survival by delaying the phenotype switch, akin to epithelial-to-mesenchymal transition (EMT), which transforms initially pigmented tumors into highly aggressive unpigmented tumors. Conclusions: Our results confirm TGFβ1 as the relevant isoform to target for cancer therapy, not only in combination with checkpoint inhibitors, but also with other immunotherapies such as cancer vaccines. Moreover, TGFβ1 blockade can also act as a monotherapy, through a tumor-intrinsic effect blocking the EMT-like transition. Because human melanomas that resist therapy often express a gene signature that links TGFβ1 with EMT-related genes, these results support the clinical development of TGFβ1-specific mAbs in melanoma.
MeSH term(s)	Animals ; Antibodies, Neutralizing/pharmacology ; Antineoplastic Agents, Immunological/pharmacology ; Cancer Vaccines/immunology ; Cancer Vaccines/pharmacology ; Cell Line, Tumor ; Colorectal Neoplasms/drug therapy ; Colorectal Neoplasms/immunology ; Colorectal Neoplasms/metabolism ; Colorectal Neoplasms/pathology ; Epithelial-Mesenchymal Transition/drug effects ; Female ; Male ; Melanoma/drug therapy ; Melanoma/immunology ; Melanoma/metabolism ; Melanoma/pathology ; Mice, Inbred BALB C ; Mice, Transgenic ; Skin Neoplasms/drug therapy ; Skin Neoplasms/immunology ; Skin Neoplasms/metabolism ; Skin Neoplasms/pathology ; Transforming Growth Factor beta1/antagonists & inhibitors ; Transforming Growth Factor beta1/immunology ; Transforming Growth Factor beta1/metabolism ; Transforming Growth Factor beta3/antagonists & inhibitors ; Transforming Growth Factor beta3/immunology ; Transforming Growth Factor beta3/metabolism ; Tumor Microenvironment ; Mice
Chemical Substances	Antibodies, Neutralizing ; Antineoplastic Agents, Immunological ; Cancer Vaccines ; Tgfb1 protein, mouse ; Tgfb3 protein, mouse ; Transforming Growth Factor beta1 ; Transforming Growth Factor beta3
Language	English
Publishing date	2021-02-26
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2719863-7
ISSN	2051-1426 ; 2051-1426
ISSN (online)	2051-1426
ISSN	2051-1426
DOI	10.1136/jitc-2020-001798
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Article ; Online: T Cell-Mediated Targeted Delivery of Anti-PD-L1 Nanobody Overcomes Poor Antibody Penetration and Improves PD-L1 Blocking at the Tumor Site.

Petit, Pierre-Florent / Bombart, Raphaële / Desimpel, Pierre-Hubert / Naulaerts, Stefan / Thouvenel, Laurie / Collet, Jean-François / Van den Eynde, Benoit J / Zhu, Jingjing

Cancer immunology research

2022 Volume 10, Issue 6, Page(s) 713–727

Abstract: Monoclonal antibodies (mAbs) blocking immune checkpoints such as programmed death ligand 1 (PD-L1) have yielded strong clinical benefits in many cancer types. Still, the current limitations are the lack of clinical response in a majority of patients and ... ...

Abstract	Monoclonal antibodies (mAbs) blocking immune checkpoints such as programmed death ligand 1 (PD-L1) have yielded strong clinical benefits in many cancer types. Still, the current limitations are the lack of clinical response in a majority of patients and the development of immune-related adverse events in some. As an alternative to PD-L1-specific antibody injection, we have developed an approach based on the engineering of tumor-targeting T cells to deliver intratumorally an anti-PD-L1 nanobody. In the MC38-OVA model, our strategy enhanced tumor control as compared with injection of PD-L1-specific antibody combined with adoptive transfer of tumor-targeting T cells. As a possible explanation for this, we demonstrated that PD-L1-specific antibody massively occupied PD-L1 in the periphery but failed to penetrate to PD-L1-expressing cells at the tumor site. In sharp contrast, locally delivered anti-PD-L1 nanobody improved PD-L1 blocking at the tumor site while avoiding systemic exposure. Our approach appears promising to overcome the limitations of immunotherapy based on PD-L1-specific antibodies.
MeSH term(s)	Antibodies, Monoclonal/pharmacology ; Antibodies, Monoclonal/therapeutic use ; B7-H1 Antigen ; Humans ; Immunotherapy ; Neoplasms/drug therapy ; T-Lymphocytes
Chemical Substances	Antibodies, Monoclonal ; B7-H1 Antigen
Language	English
Publishing date	2022-04-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2732489-8
ISSN	2326-6074 ; 2326-6066
ISSN (online)	2326-6074
ISSN	2326-6066
DOI	10.1158/2326-6066.CIR-21-0801
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Article ; Online: Navigating Critical Challenges Associated with Immunopeptidomics-Based Detection of Proteasomal Spliced Peptide Candidates.

Lichti, Cheryl F / Vigneron, Nathalie / Clauser, Karl R / Van den Eynde, Benoit J / Bassani-Sternberg, Michal

Cancer immunology research

2022 Volume 10, Issue 3, Page(s) 275–284

Abstract: Within the tumor immunology community, the topic of proteasomal spliced peptides (PSP) has generated a great deal of controversy. In the earliest reports, careful biological validation led to the conclusion that proteasome-catalyzed peptide splicing was ... ...

Abstract	Within the tumor immunology community, the topic of proteasomal spliced peptides (PSP) has generated a great deal of controversy. In the earliest reports, careful biological validation led to the conclusion that proteasome-catalyzed peptide splicing was a rare event. To date, six PSPs have been validated biologically. However, the advent of algorithms to identify candidate PSPs in mass spectrometry data challenged this notion, with several studies concluding that the frequency of spliced peptides binding to MHC class I was quite high. Since this time, much debate has centered around the methodologies used in these studies. Several reanalyses of data from these studies have led to questions about the validity of the conclusions. Furthermore, the biological and technical validation that should be necessary for verifying PSP assignments was often lacking. It has been suggested therefore that the research community should unite around a common set of standards for validating candidate PSPs. In this review, we propose and highlight the necessary steps for validation of proteasomal splicing at both the mass spectrometry and biological levels. We hope that these guidelines will serve as a foundation for critical assessment of results from proteasomal splicing studies.
MeSH term(s)	Mass Spectrometry ; Peptides ; Proteasome Endopeptidase Complex/chemistry ; Proteasome Endopeptidase Complex/metabolism
Chemical Substances	Peptides ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2022-02-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2732489-8
ISSN	2326-6074 ; 2326-6066
ISSN (online)	2326-6074
ISSN	2326-6066
DOI	10.1158/2326-6066.CIR-21-0727
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