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Human cytomegalovirus (HCMV) antigenic epitopes are specific molecular regions on viral proteins recognized by the host immune system, serving as the primary targets for vaccines and therapeutic antibodies (Source: PubMed, PMID: 31601010). The most critical epitopes for neutralizing antibodies are located on surface glycoprotein complexes, particularly Glycoprotein B (gB) and the Pentameric Complex (gH/gL/UL128/UL130/UL131A), which are essential for viral entry into epithelial, endothelial, and myeloid cells (Source: UniProt, P06473). Additionally, internal proteins such as phosphoprotein 65 (pp65/UL83) and Immediate-Early 1 (IE1/UL123) provide dominant epitopes for T-cell mediated immunity, which is crucial for controlling viral replication and maintaining latency (Source: NIH, "Cytomegalovirus (CMV) and Congenital CMV Infection"). In clinical development, these epitopes are targeted by passive immunization strategies using hyperimmune globulin and experimental monoclonal antibodies like RG7667, as well as active immunization efforts including the mRNA-1647 vaccine (Source: Moderna, mRNA-1647 Product Pipeline). Understanding the diversity and conservation of these epitopes is vital for developing broad-spectrum therapeutics against the various strains of HCMV that cause severe disease in neonates and immunocompromised individuals.
Neutralization of viral entry by blocking glycoprotein-mediated fusion with host cell membranes and induction of cellular immune responses (CD4+ and CD8+ T-cell activation) to clear infected cells.
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