Candida species protein–derived peptide bound to human leukocyte antigen (HLA) class I or class II (Candida-pMHC)

The Candida species protein–derived peptide bound to human leukocyte antigen (HLA) class I or class II is a molecular complex essential for the adaptive immune system's ability to recognize and eliminate fungal pathogens. This complex is formed when Candida-derived proteins, such as the immunodominant MP65 or secreted aspartyl proteinases (Saps), are processed into short peptides and loaded onto HLA molecules within host cells (Bacher et al., 2014). These complexes are then displayed on the cell surface, where they serve as the specific ligands for T-cell receptors (TCRs) on CD4+ or CD8+ T cells (Pietrella et al., 2001). In clinical settings, this complex is a critical target for adoptive T-cell therapies and peptide-based vaccines aimed at restoring antifungal immunity in immunocompromised patients, such as those undergoing hematopoietic stem cell transplantation (Papadopoulou et al., 2016). The therapeutic efficacy of targeting these complexes depends heavily on the patient's HLA genotype, as the specific peptide presented is determined by the binding affinity of the HLA allele's groove. Challenges in targeting this complex include the high diversity of HLA alleles across the human population and the potential for T-cell cross-reactivity with self-antigens, which could lead to adverse inflammatory or autoimmune responses.

Other names

Candida-HLA complexCandida peptide-MHC complexCandida pMHCCandida antigen-HLA complexCandida epitope-HLA complex

T-cell receptor (TCR) mediated recognition and subsequent activation of cytotoxic or helper T-cell responses against Candida-infected cells.