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Human cytomegalovirus (HCMV) virion surface antigens are a collection of glycoproteins located on the viral envelope that are essential for the virus's ability to infect host cells [1.1.2, 1.1.5]. These antigens include glycoprotein B (gB), which acts as the primary fusogen, and the gH/gL complex, which associates with other proteins to form the trimeric (gH/gL/gO) and pentameric (gH/gL/UL128/UL130/UL131A) complexes [1.2.1, 1.2.2]. These complexes determine the virus's broad cell tropism by interacting with specific host receptors, such as PDGFRα on fibroblasts and Neuropilin-2 on epithelial and endothelial cells [1.2.2, 1.2.4]. In the context of disease, these antigens are the primary targets of the host's neutralizing antibody response and are critical for the pathogenesis of HCMV-related conditions, including congenital birth defects and severe infections in immunocompromised patients [1.1.2, 1.1.3]. Therapeutically, they are the focus of vaccine development (e.g., mRNA-1647) and passive immunization strategies using hyperimmune globulins or monoclonal antibodies (e.g., Sevirumab) [1.2.1, 1.3.2, 1.3.3]. Drugs targeting these antigens work by neutralizing the virus, thereby preventing its entry into cells and subsequent replication [1.3.3].
Neutralization of viral entry by blocking attachment, receptor binding, or membrane fusion between the viral envelope and the host cell membrane.
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