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Aspergillus spp.-derived peptide–Human Leukocyte Antigen (HLA) complexes are molecular assemblies consisting of short fungal protein fragments (antigens) bound within the peptide-binding groove of HLA molecules on the surface of host cells. These complexes are essential for the recognition of Aspergillus species, such as Aspergillus fumigatus, by the cellular arm of the immune system, particularly T-cell receptors (TCRs) on CD4+ and CD8+ T cells (Stuehler et al., 2015). In the context of invasive aspergillosis, which primarily affects immunocompromised individuals, these complexes serve as the primary targets for adoptive T-cell therapies and experimental vaccines (Bacher et al., 2014). Therapeutic strategies involve the administration of ex vivo expanded Aspergillus-specific T cells that recognize these specific peptide-HLA combinations to induce fungal clearance and provide protective immunity (Papadopoulou et al., 2014). Identifying immunodominant peptides from fungal proteins like Crf1, Gel1, and Sod1 that are presented by common HLA alleles is a key area of research for developing standardized "off-the-shelf" cellular products (Göttlich et al., 2023). Targeting these complexes aims to restore or enhance the host's antifungal immunity, providing a precise mechanism to clear the pathogen while minimizing damage to healthy tissues.
T-cell receptor (TCR) mediated recognition and subsequent activation of cytotoxic or helper T-cell responses against fungal-infected cells.
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