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Cytomegalovirus (CMV) peptide-Major Histocompatibility Complex (pMHC) molecules are specialized cell-surface structures that present viral protein fragments to the immune system. These complexes typically consist of immunodominant peptides derived from CMV proteins like pp65 (UL83) or IE1 (UL123) bound to MHC Class I or II molecules [1][2]. Their primary biological function is to serve as a signal for T-cell recognition; specifically, CD8+ cytotoxic T cells identify these pMHC complexes via their T-cell receptors (TCRs), initiating the destruction of the infected cell [3]. In clinical settings, these complexes are the primary targets for adoptive T-cell therapies and vaccines aimed at restoring or enhancing CMV-specific immunity in immunocompromised patients, such as those undergoing hematopoietic stem cell or solid organ transplantation [4][5]. However, CMV has evolved sophisticated mechanisms to evade this detection by downregulating MHC expression, and therapeutic interventions must also account for potential cross-reactivity with host self-antigens [6][7]. Sources: [1] Wills et al. (1996) J Virol; [2] Reddehase (2002) Nat Rev Immunol; [3] Stern-Ginossar et al. (2012) Science; [4] Papadopoulou et al. (2013) Sci Transl Med; [5] Atara Biotherapeutics Pipeline; [6] Hansen et al. (2013) Science; [7] Linette et al. (2013) Blood.
Recognition by T-cell receptors (TCRs) on CD8+ or CD4+ T cells, or by TCR-like therapeutic molecules, which triggers an immune response leading to the apoptosis or lysis of the CMV-infected host cell.
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