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Human cytomegalovirus (HCMV) surface glycoproteins are essential structural proteins located on the viral envelope and the surface of infected cells, serving as the primary mediators of viral entry and cell-to-cell spread (PMID: 25605940). The most prominent of these include glycoprotein B (gB), the gH/gL complex, and the pentameric complex (gH/gL/UL128/UL130/UL131A), which facilitate attachment and fusion with various host cell types, including epithelial and endothelial cells (UniProt P06473, P12824). HCMV is a major cause of morbidity in immunocompromised individuals and is the leading infectious cause of congenital abnormalities worldwide (CDC, 2022). These surface antigens are the principal targets for the host's neutralizing antibody response, making them central to the design of prophylactic vaccines and monoclonal antibody therapies (PMID: 31664534). While traditional antivirals like ganciclovir target viral DNA replication, therapies directed at surface glycoproteins aim to prevent the initial infection of host cells or limit the spread of the virus within the body. Current clinical efforts include the development of mRNA vaccines and monoclonal antibodies that specifically bind these glycoproteins to neutralize the virus (Moderna, 2023; PMID: 33168513).
Therapeutic agents targeting these glycoproteins primarily function through viral neutralization, where antibodies bind to the glycoproteins to prevent the virus from attaching to or fusing with host cell membranes (PMID: 25605940). Additionally, these antigens serve as targets for antibody-dependent cellular cytotoxicity (ADCC) and complement-mediated lysis, marking infected cells for destruction by the host immune system (PMID: 30108114).
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