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Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

ABSTRACT: Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

PROVIDER: PRJNA982738 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR24895132_1.fastq.gz	Fastqsanger.gz
	SRR24895132_2.fastq.gz	Fastqsanger.gz
	SRR24895133_1.fastq.gz	Fastqsanger.gz
	SRR24895133_2.fastq.gz	Fastqsanger.gz
	SRR24895134_1.fastq.gz	Fastqsanger.gz

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Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

Project description:Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

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Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

Project description:Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

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Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-06-17 | GSE234676 | GEO

Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

Project description:We performed bulk RNAsequencing of neutrophils isolated from whole blood treated with CD20-TCB to study the early kinetics of cytokine release in neutrophils.

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Dissecting the mechanisms underlying the Cytokine Release Syndrome (CRS) mediated by T Cell Bispecific Antibodies

Project description:We performed bulk RNAseq of HUVECs exposed to cytokine-rich supernatant from T cell dependent cytotoxicity assay with CEA-TCB or DP47-TCB (untargeted-TCB; negative control) to study their activation and contribution to cytokine release.

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Bispecific antibodies increase the therapeutic window of CD40 agonists through selective dendritic cell targeting

Project description:Therapeutic use of agonistic anti-CD40 antibodies is a potentially powerful approach for activating the immune response to eradicate tumors. However, the translation of this approach to clinical practice has been significantly restricted due to the severe dose-limiting toxicities observed in multiple clinical trials. Here, we demonstrate that conventional type-1 dendritic cells are essential for triggering antitumor immunity but not toxicity by CD40 agonists, while macrophages, platelets, and monocytes lead to the toxic events. Therefore, we designed bispecific antibodies that target CD40 activation preferentially to dendritic cells. These bispecific reagents demonstrate a superior safety profile compared to their parental CD40 monospecific antibody, while triggering potent anti-tumor activity. We suggest such cell-selective bispecific agonistic antibodies as a drug platform to bypass the dose-limiting toxicities of anti-CD40, and of additional types of agonistic antibodies used for cancer immunotherapy.

2021-12-12 | GSE184009 | GEO

Simultaneous substrate and ubiquitin modification recognition by bispecific antibodies allows detection of ubiquitinated RIP1 and RIP2

Project description:Ubiquitination is crucial for the dynamic regulation of diverse signaling pathways. To enhance understanding of ubiquitination mediated signaling, we generated a new class of bispecific antibodies which combine recognition of ubiquitination substrates and specific polyubiquitin linkages. RIP1-K63 or RIP1-linear (Lin) linkage polyubiquitin bispecific antibodies can detect linkage-specific RIP1 ubiquitination in cells and in tissues, and also reveal RIP1 ubiquitination by immunofluorescence. In a similar fashion, RIP2 ubiquitination with K63 or linear linkages can be specifically detected with RIP2-K63 and RIP2-Lin bispecific antibodies. Furthermore, using RIP2-K63 and RIP2- Lin bispecific antibodies we examined IBD patient samples and found prominent K63- linked and linear RIP2 ubiquitination in ulcerative colitis and Crohn's disease patient samples. We also developed a bispecific antibody (K63-Lin) that can simultaneously recognize K63-linked and linear ubiquitination in a variety of signaling pathways. Collectively, these bispecific antibodies provide a novel conceptual paradigm for potential future development of inflammatory markers.

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Schropp2019 - Target-Mediated Drug Disposition Model for Bispecific Antibodies

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Project description:CD3-bispecific antibodies represent an important therapeutic strategy in oncology. These molecules work by redirecting cytotoxic T cells to antigen-bearing tumor cells. Although CD3-bispecific antibodies have been developed for several clinical indications, cases of cancer-derived resistance are an emerging limitation to the more generalized application of these molecules. Here, we devised whole-genome CRISPR screens to identify cancer resistance mechanisms to CD3-bispecific antibodies across multiple targets and cancer types. By validating the screen hits, we found that deficiency in IFNγ signaling has a prominent role in cancer resistance. Interestingly, IFNγ functions by stimulating the expression of T cell killing-related molecules in a cell type-specific manner. Additionally, by assessing resistance to the clinical CD3-bispecific antibody flotetuzumab, we identified core fucosylation as a novel and critical pathway to regulate flotetuzumab binding to the CD123 antigen. Disruption of this pathway resulted in significant resistance to flotetuzumab treatment. Moreover, proper fucosylation of CD123 is required for its normal biological functions. In order to treat the resistance associated with fucosylation loss, flotetuzumab in combination with an alternative targeting CD3-bispecific antibody demonstrated superior efficacy. Together, our study reveals multiple mechanisms that can be targeted to enhance the clinical potential of current and future T cell engaging CD3-bispecific antibody therapies.

2020-11-12 | GSE159547 | GEO

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Project description:The COVID-19 pandemic prompted an unprecedented effort to develop effective countermeasures against SARS-CoV-2. While efficacious vaccines and certain therapeutic monoclonal antibodies are available, here, we report the development, cryo-EM structures and functional analyses of distinct potent monoclonal antibodies (mAbs) that neutralize SARS-CoV-2 and its variant B.1.351. We established a platform for rapid identification of highly potent and specific SARS-CoV-2-neutralizing antibodies by high-throughput B cell receptor single cell sequencing of spike receptor binding domain immunized animals. We identified two highly potent and specific SARS-CoV-2 neutralizing mAb clones that have single-digit nanomolar affinity and low-picomolar avidity. We also generated a bispecific antibody of these two lead clones. The lead monospecific and bispecific antibodies showed strong neutralization ability against prototypical SARS-CoV-2 and the highly contagious South African variant B.1.351 that post a further risk of reducing the efficacy of currently available therapeutic antibodies and vaccines. The lead mAbs showed potent in vivo efficacy against authentic SARS-CoV-2 in both prophylactic and therapeutic settings. We solved five cryo-EM structures at ~3 resolution of these neutralizing antibodies in complex with the ectodomain of the prefusion spike trimer, and revealed the molecular epitopes, binding patterns and conformations between the antibodies and spike RBD, which are distinct from existing antibodies. Our recently developed antibodies expand the repertoire of the toolbox of COVID-19 countermeasures against the SARS-CoV-2 pathogen and its emerging variants.

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