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Translation dysregulation in cancer as a source for targetable antigens.

ABSTRACT: Translation dysregulation in cancer as a source for targetable antigens.

PROVIDER: PRJNA1139766 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29979703.fastq.gz	Fastqsanger.gz
	SRR29979704.fastq.gz	Fastqsanger.gz
	SRR29979705.fastq.gz	Fastqsanger.gz
	SRR29979706.fastq.gz	Fastqsanger.gz
	SRR29979707.fastq.gz	Fastqsanger.gz

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Translation dysregulation in cancer as a source for targetable antigens

Project description:Aberrant peptides presented by major histocompatibility complex (MHC) molecules are targets for tumor eradication, as these peptides can be recognized as foreign by T cells. Protein synthesis in malignant cells is dysregulated, resulting in the production of non-canonical aberrant peptides. We hypothesized that inducing translation aberrations in cancers might reveal neopeptides that can be exploited for T cell-based therapies. To explore this hypothesis, we disrupted translation fidelity by silencing TYW2, a tRNA-yW synthesizing Protein 2 that supports reading-frame maintenance. Using ribosome profiling coupled with immunopeptidomics, we uncover a large set of out-of-frame peptides in TYW2 KO cells and demonstrate that these aberrant peptides are highly immunogenic. Furthermore, we show that Tyw2 loss leads to increased immunogenicity of melanoma tumors in vivo, mediated through cytotoxic T cell activity. Importantly, treatment of Tyw2 KO tumor-bearing mice with anti-PD1 checkpoint blockade therapy further reduces tumor growth, and its reduced expression is associated with increased response to checkpoint blockade therapy in patients. Together, our data shows that defects in translation fidelity indeed contribute to tumor immunogenicity and suggests that they can be harnessed for cancer immunotherapy modalities.

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Translation dysregulation in cancer as a source for targetable antigens.

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Project description:Purpose: Tumor-specific antigens (TSAs) represent ideal targets for cancer immunotherapy, but very few of them have been identified. Therefore, the goal of this study was to develop a novel approach, combining RNA-Sequencing and mass spectrometry, to enlarge the landscape of actionable TSAs in seven human primary samples, namely 4 B-ALL and 3 lung tumor biopsies. Methods: We performed RNA-Sequencing on each primary tumor sample (unreplicated) with the Illumina HiSeq200. Using those RNA-Sequencing data to build a global cancer database for each sample, we performed a transcriptomic-informed mass spectrometry analysis of their MHC I-associated peptides to identify TSAs. Results: We identified a total of 30 TSAs, 90% of which derived from allegedly non-coding regions and would have been missed by standard approaches. Moreover, most of these TSAs derived from non-mutated yet cancer-restricted transcripts that can be shared by multiple tumors. Conclusions: In conclusion, the strategy reported herein is readily applicable to human tumors and should considerably enlarge the landscape of actionable TSAs.

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