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Antigen processing and presentation is the process by which protein antigen is ingested by an antigen-presenting cell (APC), partially digested into peptide fragments and then displayed on the surface of the APC associated with an antigen-presenting molecule such as MHC class I or MHC class II, for recognition by certain lymphocytes such as T cells.
Cathepsin L, a lysosomal protease, is critical for thymic epithelial cell function, particularly in CD4+ T cell selection, TCR repertoire diversity and the regulation of peripheral immune responses.
Klein and colleagues show that the lysosomal cysteine protease cathepsin L shapes the diversity and optimizes the fitness of clones that enter the CD4+ T cell repertoire.
Development of T cells in the thymus results in small populations of innate like T cells. Here the authors characterise a population of innate-like T cells in mice engineered to enable MHC class I expression in the double positive stage which allows a population of PLZF expressing PILT innate-like T cells to develop.
Sequence-based algorithms to identify T cell antigens often miss targets that are activating the immune response. Here authors show that a computational method they developed, which uses atomic level features as input, can identify antigens that trigger cytokine release in cognate T cells.
Immune tolerance to dietary antigens is mediated by a circuit of dedicated antigen-presenting cells and T cells, ensuring protective effector responses without compromising the overall strategy of tolerance that ensures safe food consumption.
Cathepsin L, a lysosomal protease, is critical for thymic epithelial cell function, particularly in CD4+ T cell selection, TCR repertoire diversity and the regulation of peripheral immune responses.
A healthy immune system is tolerant to self-antigens while maintaining responsiveness to foreign threats. Co-expression of the inhibitory receptors PD-1 and CD73 regulates tolerance by restricting the expansion of auto-reactive CD4+ T cells independently of thymic selection.
A method for designing high-affinity, specific binders to peptide–MHC complexes may improve the next generation of antigen-specific T cell-based therapeutics.
