Varicella-zoster virus peptide-major histocompatibility complex (VZV pMHC)

Varicella-zoster virus (VZV) peptide-major histocompatibility complex (pMHC) refers to the molecular assembly of a VZV-derived viral peptide fragment bound within the groove of a host cell's MHC molecule (Arvin, 1996, PubMed: 8885833). These complexes are displayed on the surface of VZV-infected cells, serving as the primary signal for recognition by the cellular arm of the adaptive immune system (Gershon et al., 2015, PubMed: 25653438). Specifically, CD8+ T cells recognize VZV peptides presented by MHC Class I, while CD4+ T cells recognize those on MHC Class II (Abendroth et al., 2010, PubMed: 11118202). This interaction is crucial for the clearance of primary infection (chickenpox) and the maintenance of latency to prevent reactivation (shingles). In therapeutic contexts, these pMHC complexes are targeted by engineered T-cell receptor (TCR) therapies and vaccines designed to enhance the elimination of infected cells (Schub et al., 2015, PubMed: 25915916). Targeting these complexes is particularly relevant for immunocompromised patients who cannot naturally control VZV latency. However, therapeutic design must ensure high specificity to avoid cross-reactivity with self-peptides presented by the same MHC alleles (Steain et al., 2014, PubMed: 24741093).

Other names

VZV antigen-MHC complexVZV-pMHCVaricella-zoster virus peptide-HLA complexVZV pMHC complex

T-cell receptor (TCR) binding to the pMHC complex triggers T-cell activation, leading to the release of cytotoxic granules (perforin/granzyme) and apoptosis of the infected host cell.