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Human cytomegalovirus (HCMV) surface glycoprotein antigens are essential viral envelope proteins that mediate the complex process of virus attachment, signaling, and membrane fusion with host cells (PubMed: 28232530). The primary targets for therapeutic development include glycoprotein B (gB), which functions as the class III viral fusion protein, and the gH/gL complex, which often associates with accessory proteins like gO or the UL128-131A subunits to form the pentameric complex (PubMed: 26311877). These glycoproteins are the dominant targets of the neutralizing antibody response during natural infection, making them ideal candidates for vaccine design and monoclonal antibody therapy (UniProt: P06473). By targeting these antigens, drugs aim to block viral entry into diverse cell types, including fibroblasts, epithelial cells, and endothelial cells, thereby preventing systemic dissemination and organ damage. Currently, passive immunization with CMV-specific hyperimmune globulin (CytoGam) is utilized in high-risk patients, while various mRNA and subunit vaccines targeting these glycoproteins, such as mRNA-1647, are undergoing clinical trials (NCT05085301). These antigens play a central role in the pathogenesis of congenital CMV and opportunistic infections in immunocompromised individuals, such as transplant recipients.
Neutralization of viral entry into host cells by blocking the interaction between viral envelope glycoproteins and host cell receptors, thereby preventing membrane fusion and viral DNA release (PubMed: 28232530).
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