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Human cytomegalovirus (HCMV) glycoprotein B (gB) and the pentameric complex (PC) are the primary surface antigens responsible for viral entry and are the leading targets for vaccine and antibody-based therapies. Glycoprotein B, encoded by the UL55 gene, is a highly conserved Class III viral fusion protein that is essential for the fusion of the viral envelope with host cell membranes across all cell types (UniProt P06473). The pentameric complex, composed of gH, gL, and the subunits UL128, UL130, and UL131A, is required for entry into epithelial, endothelial, and myeloid cells, which are critical for the virus's systemic spread and transmission (PMID: 28834383). Because the PC is the target of the most potent neutralizing antibodies found in naturally infected individuals, it is a central component of modern vaccine candidates like mRNA-1647 (Moderna). Therapeutic strategies focusing on these antigens aim to elicit or provide antibodies that block viral attachment and fusion, thereby preventing primary infection or reactivation. This is particularly vital for preventing congenital CMV infection in newborns and managing opportunistic infections in immunocompromised transplant recipients.
Neutralization of viral entry by blocking membrane fusion and cell-surface attachment through the induction or provision of antibodies targeting gB and the pentameric complex components.
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