Abstract
In the past decade, anti-tumour immune responses have been successfully exploited to improve the outcome of patients with different cancers. Significant progress has been made in taking advantage of different types of T cell functions for therapeutic purposes. Despite these achievements, only a subset of patients respond favorably to immunotherapy. Therefore, there is a need of novel approaches to improve the effector functions of immune cells and to recognize the major targets of anti-tumour immunity. A major hallmark of cancer is metabolic rewiring associated with switch of mitochondrial functions. These changes are a consequence of high energy demand and increased macromolecular synthesis in cancer cells. Such adaptations in tumour cells might generate novel targets of tumour therapy, including the generation of neoantigens. Here, we review the most recent advances in research on the immune response to mitochondrial proteins in different cellular conditions.
Highlights
The mammalian mitochondrion comprises between 1000 and 1500 proteins, the vast majority of which are encoded by the nuclear genome, whilst a small number is encoded by the mitochondrial genome [6,7]
MtDNA is anchored to the inner mitochondrial membrane (IMM) within the mitochondrial matrix, packaged into protein–DNA complexes known as ‘nucleoids’, which are principally formed by the mitochondrial transcription factor A (TFAM) [10]
The ability of the human immune system to recognize and mount an immune response against mitochondrial mutated proteins has been observed under different pathological conditions
Summary
Mitochondria are organelles with primary functions in producing energy and metabolic intermediates required for many cellular activities. Recent novel phylogenomic analyses support the theory that mitochondria originated from an alphaproteobacterial endosymbiont [2,3] During evolution, this endosymbiotic interaction gradually became further intertwined, with most mitochondrial genetic information being transferred to the nucleus. Mitochondrial proteins physically interact with other peptides produced by the nuclear genome to form respiratory chain complexes; alterations in the mtDNA sequence may modify the assembly and function of each complex [12]. Such modifications may alter cell phenotype and functions, and this paradigm is of particular interest in diseases, including cancer
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