Aspergillus-derived peptide-HLA complex (Aspergillus pHLA)

Aspergillus-derived peptides presented by patient HLA class I or II molecules represent the fundamental recognition unit for the adaptive cellular immune response against Aspergillus species, most notably Aspergillus fumigatus (Bacher et al., 2014, Cell). These complexes are formed when fungal proteins, such as Crf1, Gel1, or Asp f 1, are processed by host antigen-presenting cells and their constituent peptides are loaded onto Human Leukocyte Antigen (HLA) molecules for surface display (Stuehler et al., 2011, Journal of Infectious Diseases). HLA class I complexes typically present peptides to CD8+ cytotoxic T cells, while HLA class II complexes present to CD4+ helper T cells, which are crucial for coordinating the antifungal response through the secretion of cytokines like IFN-gamma and IL-17 (Beck et al., 2006, Blood). In clinical settings, these pHLA complexes are the primary targets for adoptive T-cell therapies, where Aspergillus-specific T cells are expanded and infused into immunocompromised patients to restore fungal immunity (Potenza et al., 2005, Blood). They also serve as the basis for experimental peptide vaccines designed to elicit protective immunity in high-risk populations, such as hematopoietic stem cell transplant recipients. Understanding the specific peptide-HLA repertoire is essential for developing precision immunotherapies that ensure robust fungal clearance while minimizing off-target reactivity.

Other names

Aspergillus antigen-HLA complexAspergillus-specific T-cell epitopesAspergillus peptide-MHC complexFungal peptide-HLA complex

T-cell receptor (TCR) mediated recognition of the peptide-HLA complex leading to T-cell activation and subsequent antifungal effector functions.