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Human leukocyte antigen (HLA) class I and class II molecules presenting cytomegalovirus (CMV)-derived peptide epitopes are essential components of the host immune response to CMV infection. These complexes consist of host-encoded HLA proteins bound to short viral peptide fragments, most commonly derived from the CMV proteins pp65 and IE1 (Source: PubMed, PMID: 28213375). Their primary biological function is to present these viral antigens to the T-cell receptors (TCRs) of CD8+ and CD4+ T lymphocytes, thereby facilitating the identification and elimination of infected cells (Source: UniProt). In immunocompromised individuals, such as transplant recipients, the failure of the immune system to recognize these HLA-peptide targets often results in CMV reactivation, leading to severe complications like pneumonia or hepatitis (Source: NIH). Therapeutic strategies targeting these complexes include adoptive T-cell therapies, such as posoleucel, which provide exogenous T cells capable of recognizing these specific epitopes to restore viral control (Source: AlloVir). Furthermore, peptide and viral-vector vaccines are being developed to enhance the presentation of these epitopes and stimulate a protective endogenous immune response (Source: PubMed, PMID: 30552139).
Recognition of the peptide-HLA complex by T-cell receptors (TCRs) on adoptive or endogenous T cells, leading to the lysis of CMV-infected cells and viral control.
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