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Evaluation of the impact of scFv on functionality and safety of 3rd generation CD123 CAR T cells

ABSTRACT: Evaluation of the impact of scFv on functionality and safety of 3rd generation CD123 CAR T cells

PROVIDER: PRJNA1066843 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27662844_1.fastq.gz	Fastqsanger.gz
	SRR27662844_2.fastq.gz	Fastqsanger.gz
	SRR27662845_1.fastq.gz	Fastqsanger.gz
	SRR27662845_2.fastq.gz	Fastqsanger.gz
	SRR27662846_1.fastq.gz	Fastqsanger.gz

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Evaluation of the impact of scFv on functionality and safety of 3rd generation CD123 CAR T cells

Project description:Chimeric Antigen Receptor T cells express an extracellular domain consisting of a single-chain fragment variable (scFv) targeting a surface tumor-associated antigen (TAA), it is important to select scFv regarding safety profile through evaluation of the efficacy/toxicity balance, especially in cases where the target antigen is also expressed on healthy cells. Here, we developed five CAR T cells targeting CD123 (CD123 CAR-T) by substituting only the scFv, looking for differences in terms of efficacy and on-target/off-tumor effects. Using in vitro models, we found that three of the five CD123 CAR-T were more cytotoxic against leukemic cells, without increasing lysis of monocytes or endothelial cells. Using the Incucyte system, we confirmed the low cytotoxicity of CD123 CAR-T on endothelial cells. Hematotoxicity evaluated by progenitor culture and CD34 cell lysis showed that two of the five CD123 CAR-T were less cytotoxic against HSC, and we confirmed in a humanized mouse model that CD123- cells were not eliminated by the CD123 CAR-T. These two CD123 CAR-T reduced tumor infiltration and increased overall survival of mice in three in vivo models of BPDCN. Moreover, in BPDCN aggressive model, bulk RNA-sequencing analysis showed that these CD123 CAR-T upregulated genes associated with cytotoxicity and activation/exhaustion a few days after the injection. Finally, we were able to produce CD123 CAR-T selected previously from patient T cells. Together, these results emphasize the importance of screening different scFv for the development of CAR-T constructs, to select the one with the optimal risk-benefit ratio for clinical development.

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Analysis of Escherichia coli CyDisCo proteome changes in response to the expression of scFv and the misfolded scFv

Project description:E. coli CyDisCo strain enables a high yield secretion of disulfide bond-containing proteins to the periplasm via Twin-arginine (Tat) pathway. Introducing two exogenous oxidases: the yeast sulfydryl oxidase (Erv1p) and human protein disulfide isomerase (PDI), the CyDisCo strain changes the cytoplasm into an oxidized environment, where the disulfide bonds can efficiently be formed. In this study, we analyzed the proteome changes upon the expression of disulfide bond-containing scFv and the misfolded scFv in the CyDisCo strain. The correctly folded protein is secreted to the periplasm, while the misfolded protein accumulates exclusively in the inclusion body fraction. We observed a high number of significant changes mostly in proteins associated with protein folding and degradation, oxidative stress, membrane transport and integrity.

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