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Human cytomegalovirus glycoprotein B (gB) is an essential class III viral fusion protein that mediates the fusion of the viral envelope with host cell membranes, enabling virus entry[1][2][4][5][6]. It is a major target of the host immune response, and antibodies targeting gB may be either neutralizing or non-neutralizing[1][2][3][7]. The HCMV pentameric complex—comprising gH, gL, and viral proteins UL128, UL130, and UL131A—enables broad cell tropism and is critical for entry into epithelial, endothelial, and myeloid cells[4]. Both gB and the pentameric complex are required for full cell entry capability; gB mediates membrane fusion, while the pentamer facilitates attachment and tropism. These proteins are major antigens considered in vaccine development and antibody therapeutics, making them validated therapeutic targets for treating or preventing HCMV infection in high-risk populations, such as immunocompromised individuals and newborns[1][3][4][5][7]. Safety concerns in targeting these molecules include the risk of non-neutralizing antibody responses, potential immune evasion through glycosylation and antigenic variation, and the challenge of achieving long-lasting and broadly protective immunity[1][2][4].
Neutralizing antibody binding to block viral entry; Inhibition of membrane fusion; Vaccine-elicited immune protection
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